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rdf:type
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rdfs:label
Hemoglobine Hemoglobin Hemoglobin Hemoglobina Hémoglobine Hemoglobin 血红蛋白 Hemoglobina Αιμοσφαιρίνη Гемоглобин Hemoglobina Hämoglobin Hemoglobino Hemoglobina Emoglobina 헤모글로빈 Hemoglobin Гемоглобін ヘモグロビン هيموغلوبين Hemoglobina Haemaglóibin
rdfs:comment
Hämoglobin (von altgriechisch αἷμα haíma, „Blut“, und lateinisch globus, „Klumpen, Ballen“), Abkürzung Hb, ist der eisenhaltige Proteinkomplex, der als Blutfarbstoff in den roten Blutkörperchen von Wirbeltieren enthalten ist, Sauerstoff bindet und diesen so im Blutkreislauf transportiert. Zum Vorkommen von Hämoglobin und ähnlicher Globine im Tierreich siehe Sauerstofftransporter. Гемоглоби́н (от др.-греч. αἷμα «кровь» + лат. globus «шар») (Hb или Hgb) — сложный железосодержащий белок животных, обладающих кровообращением, способный обратимо связываться с кислородом, обеспечивая его перенос в ткани. У позвоночных животных содержится в эритроцитах, у большинства беспозвоночных растворён в плазме крови (эритрокруорин) и может присутствовать в других тканях. Молекулярная масса гемоглобина человека — около 66,8 кДа. Молекула гемоглобина может нести до четырёх молекул кислорода. Один грамм гемоглобина может переносить до 1,34 мл кислорода. Hemoglobin (haemoglobin BrE) (from the Greek word αἷμα, haîma 'blood' + Latin globus 'ball, sphere' + -in) (/ˌhiːməˈɡloʊbɪn, ˈhɛmoʊˌ-/), abbreviated Hb or Hgb, is the iron-containing oxygen-transport metalloprotein present in red blood cells (erythrocytes) of almost all vertebrates (the exception being the fish family Channichthyidae) as well as the tissues of some invertebrates. Hemoglobin in blood carries oxygen from the respiratory organs (e.g. lungs or gills) to the rest of the body (i.e. tissues). There it releases the oxygen to permit aerobic respiration to provide energy to power functions of an organism in the process called metabolism. A healthy individual human has 12 to 20 grams of hemoglobin in every 100 mL of blood. Η αιμοσφαιρίνη είναι πρωτεΐνη του αίματος η οποία προσδένει οξυγόνο. Είναι σφαιρική και αποτελείται από τέσσερις πολυπεπτιδικές αλυσίδες ανά δύο όμοιες και τέσσερα μόρια αίμης, τα οποία είναι ενωμένα ανά ένα σε κάθε αλυσίδα. L'emoglobina (indicata con la sigla Hb, dall'inglese hemoglobin) è una proteina globulare con struttura quaternaria formata da quattro subunità. È solubile e di colore rosso (cromoproteina). È presente nei globuli rossi dei vertebrati (esclusi alcuni pesci antartici) per i quali svolge la funzione vitale di trasporto dell'ossigeno molecolare da un compartimento ad alta concentrazione di O2, il sangue arterioso, ai tessuti. ( 영화에 대해서는 헤모글로빈 (영화) 문서를 참고하십시오.) 헤모글로빈(hemoglobin, haemoglobin) 또는 혈색소(血色素)는 적혈구에서 철을 포함하는 붉은 색 단백질로, 산소를 운반하는 역할을 한다. 헤모글로빈은 산소 분압이 높은 폐에서는 산소와 잘 결합하고, 산소 분압이 낮은 체내에서는 결합하던 산소를 유리하는 성질이 있다. 분자식은 C3032H4816O872N780S8Fe4 이다. 분자식에서 설명한 것처럼 철 원자가 4개 포함되어 있기 때문에 철이 부족하면 헤모글로빈이 완전하게 기능할 수 없어 빈혈(anemia)이 일어나게 된다. Hemoglobina (gr. αἷμα haîma "krew", łac. globus "kula"), oznaczana też skrótami Hb lub HGB – czerwony barwnik krwi, białko zawarte w erytrocytach, którego zasadniczą funkcją jest transportowanie tlenu – przyłączanie go w płucach i uwalnianie w tkankach. Mutacje genu hemoglobiny prowadzą do chorób dziedzicznych: anemii sierpowatej, talasemii lub rzadkich chorób zwanych hemoglobinopatiami. Hemoglobin (zkratka Hb) je červený transportní metaloprotein červených krvinek obratlovců a některých dalších živočichů. Hlavní funkcí hemoglobinu je transport kyslíku z plic nebo žaber do tkání a opačným směrem odstraňování oxidu uhličitého z tkání do plic. V aktivních erytrocytech savců hemoglobin tvoří 35 % obsahu. Průměrné množství hemoglobinu v jednom erytrocytu je 28–32 pg. ヘモグロビン(hemoglobin、Hb、血色素)とは、ヒトを含む全ての脊椎動物や一部のその他の動物の血液中に見られる赤血球の中に存在するタンパク質である。酸素分子と結合する性質を持ち、肺から全身へと酸素を運搬する役割を担っている。赤色素であるヘムを持っているため赤色を帯びている。 以下では、特にことわりのない限り、ヒトのヘモグロビンについて解説する。 血红蛋白(Hemoglobin,縮寫 Hb、Hgb)又稱血红素,俗稱血色素,是高等生物体内红色含铁的携氧结合蛋白。血红蛋白的结构为异源四聚体,由2对珠蛋白组成,每个珠蛋白结合1个血基質。 哺乳动物的一个血红蛋白分子,可以结合最多四个氧分子。可以用平均細胞血紅蛋白濃度測出濃度。 A Hemoglobina (frequentemente abreviada como Hb) é uma metaloproteína (iões metálicos na estrutura) que contém ferro, presente nos glóbulos vermelhos (eritrócitos) e que permite o transporte de oxigénio pelo sistema circulatório. Composta de 4 moléculas proteicas de estrutura terciária e 4 grupamentos heme que contém o ferro, cada íon ferro é capaz de se ligar frouxamente a uma molécula de oxigênio. Hemoglobin adalah (protein yang mengandung zat besi) di dalam sel darah merah yang berfungsi sebagai pengangkut oksigen dari paru-paru ke seluruh tubuh, pada mamalia dan hewan lainnya. Hemoglobin juga pengusung karbon dioksida kembali menuju paru-paru untuk dihembuskan keluar tubuh. Molekul hemoglobin terdiri dari , , dan empat gugus heme, suatu molekul organik dengan satu atom besi. Mutasi pada gen protein hemoglobin mengakibatkan suatu golongan penyakit menurun yang disebut , di antaranya yang paling sering ditemui adalah anemia sel sabit dan talasemia. L'hémoglobine, couramment symbolisée Hb, parfois Hgb, est un pigment respiratoire (de la famille moléculaire des métalloprotéines, ici contenant du fer) présent essentiellement dans le sang des vertébrés, au sein de leurs globules rouges, ainsi que dans les tissus de certains invertébrés. Elle a pour fonction de transporter l'oxygène O2 depuis l'appareil respiratoire (poumons, branchies) vers le reste de l'organisme. La quantité d'hémoglobine est un paramètre mesuré lors d'un hémogramme. Hemoglobin, ofta förkortat Hb, ibland Hgb, är ett protein som finns i röda blodkroppar hos människan och många djur. Hemoglobinet står för syrgastransporten i blodet. I äldre litteratur stavas det ibland hämoglobin. Hemoglobinet transporterar syrgas från lungorna ut till kroppens övriga vävnader, exempelvis musklerna och hjärnan. Där lämnar hemoglobinet sitt syre och plockar upp avfallsprodukten koldioxid för att frakta den tillbaka till lungorna, där den lämnar kroppen. هيموغلوبين أو هيموجلوبين أو خضاب الدم أو اليحمور (بالإنجليزية: Haemoglobin)‏ هو بروتين محمول داخل خلايا الدم الحمراء ويحتوي على ذرات الحديد (Fe). يلتقط الأوكسجين في الرئتين ويسلّمه إلى الأنسجة للحفاظ على حياة الجسم. يتكون الهيموجلوبين من بروتينين متماثلين ملتصقين ببعضهما بعضا. يجب تواجد كِلا البروتينين ليستطيع الهيموجلوبين تحميل وإعطاء الأوكسجين لخلايا الجسم. أحد البروتينين يدعى ألفا، والآخر بيتا. قبل الولادة، لا يتم إنتاج بروتين بيتا. لكن يوجد بروتين آخر يحل مكانه يسمى غاما، وهو لا يوجد إلا في طور الجنين، ويعمل كبديل للبيتا حتى وقت الولادة. Hemoglobino estas la feroentena ruĝkolorigaĵo en la eritrocitoj de la vertebruloj. La hemoglobino konstruiĝas el kvar feroligaj hemoj kiel prosteta grupo kaj el kiel proteina parto. Hemoglobino ebligas la transporton de oksigeno (O2, kaptita de la pulmoj aŭ brankoj dum enspiro de vertebruloj), al histoĉeloj, liverante al ili energion por la bonfunkcio de la organismo (Vd metabolismo-n). Aliflanke hemoglobino ebligas ankaŭ la transporton de karbona dioksido (CO2), produktita de tiaj ĉeloj, kiu estas emisiita al aero per la pulmoj aŭ brankoj dum elspiro. Karakterizaĵoj de la hemoglobin-molekulo: Hemoglobina odolaren heteroproteina da, ugaztun eta beste ornodun batzuen globulu gorrietan dagoena. Bere eginkizun nagusia oxigenoaren garraioa da, arnas aparatutik gorputzeko ehunetara. Pigmentu gorria da, eta odolari gorri kolorea ematen dio. Bere pisu molekularra 64.000 Daltonekoa da. Hemoglobina, heteroproteina guztien antzera, talde proteikoz (proteinaz) eta talde prostetikoz (molekula ez-proteikoz) osatuta dago. Hemoglobinaren talde prostetikoa eraztun tetrapirrolikoa da, erdian burdin atomoa duena (ikusi irudia). Talde prostetikoari hemo taldea deritzo. Hb + 4O2 -> Hb(O2)4 Гемоглобін (від грец. αἷμα, трансліт. haîma — кров і лат. globus — куля + -ін), скорочено Hb або Hgb — залізовмісний киснево-транспортний металопротеїн в еритроцитах (червоних кров'яних тільцях) більшості хребетних (за винятком родини риб Білокрівкові) та тканинах деяких безхребетних. Гемоглобін у крові переносить кисень від дихальних органів (наприклад, легень або зябер) до решти тіла (тобто тканин). Там він вивільняє кисень, щоби забезпечити аеробне дихання, яке своєю чергою забезпечує енергію задля виконання функцій організму в процесі, який має назву обмін речовин. У здоровому ораганізмі на 100 мл крові міститься від 12 до 20 грам гемоглобіну. La hemoglobina es una hemoproteína de la sangre, de masa molecular de 64 000 g/mol (64 kDa), de color rojo característico, que transporta el dioxígeno (comúnmente llamado oxígeno), O2, desde los órganos respiratorios hasta los tejidos, el dióxido de carbono, CO2, desde los tejidos hasta los pulmones que lo eliminan y también participa en la regulación de pH de la sangre, en vertebrados y algunos invertebrados. Is éard is haemaglóibin ann ná próitéin ina bhfuil an haem-mhóilín, ina bhfuil adamh iarainn lárnach, a iompraíonn ocsaigin sa bhfuil. Tá dhá roinn sa bhfuil agus an toirt chéanna iontu: na cealla bána is dearga (na heiritricítí), agus an fuilphlasma. Sna heiritricítí atá an haemaglóibin lonnaithe. I dtimthriall amháin d'imshruthú na fola, agus an fhuil ag rith trí na ribeadáin fola sna scamhóga, idirleathann an ocsaigin isteach inti ó na hailbheolais, agus tagann dath dearg ar an bhfuil athnuaite seo. Hemoglobine (Hb) is een gespecialiseerd eiwit dat het transport van zuurstof (O2) en koolstofdioxide (CO2) door het bloed van veel dieren verzorgt. Rode bloedcellen zijn voor 1/3 deel gevuld met hemoglobine. IJzer in het hemoglobine geeft bloed zijn rode kleur. De verbinding van zuurstof en hemoglobine (oxyhemoglobine) is lichtrood. L'hemoglobina (abreujada com a Hb o Hgb) és la proteïna que transporta l'oxigen i conté ferro. Es troba als glòbuls vermells dels vertebrats, i als teixits d'alguns invertebrats. En mamífers, la proteïna constitueix aproximadament un 97% del contingut sec del glòbul vermell, i al voltant d'un 35% del contingut total (incloent-hi aigua). L'hemoglobina transporta oxigen des dels pulmons o brànquies fins a la resta del cos (i.e. els teixits) on allibera l'oxigen per a l'ús de les cèl·lules. També té més varietat de funcions transport de gas i modulació que varien d'espècie a espècie, i són bastant diversos en alguns invertebrats. Per exemple, l'hemoglobina transporta CO₂ de tornada des dels teixits fins als pulmons.
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dbo:abstract
A Hemoglobina (frequentemente abreviada como Hb) é uma metaloproteína (iões metálicos na estrutura) que contém ferro, presente nos glóbulos vermelhos (eritrócitos) e que permite o transporte de oxigénio pelo sistema circulatório. Composta de 4 moléculas proteicas de estrutura terciária e 4 grupamentos heme que contém o ferro, cada íon ferro é capaz de se ligar frouxamente a uma molécula de oxigênio. Hemoglobin (zkratka Hb) je červený transportní metaloprotein červených krvinek obratlovců a některých dalších živočichů. Hlavní funkcí hemoglobinu je transport kyslíku z plic nebo žaber do tkání a opačným směrem odstraňování oxidu uhličitého z tkání do plic. V aktivních erytrocytech savců hemoglobin tvoří 35 % obsahu. Průměrné množství hemoglobinu v jednom erytrocytu je 28–32 pg. Гемоглобін (від грец. αἷμα, трансліт. haîma — кров і лат. globus — куля + -ін), скорочено Hb або Hgb — залізовмісний киснево-транспортний металопротеїн в еритроцитах (червоних кров'яних тільцях) більшості хребетних (за винятком родини риб Білокрівкові) та тканинах деяких безхребетних. Гемоглобін у крові переносить кисень від дихальних органів (наприклад, легень або зябер) до решти тіла (тобто тканин). Там він вивільняє кисень, щоби забезпечити аеробне дихання, яке своєю чергою забезпечує енергію задля виконання функцій організму в процесі, який має назву обмін речовин. У здоровому ораганізмі на 100 мл крові міститься від 12 до 20 грам гемоглобіну. У ссавців хромопротеїн становить близько 96 % сухого вмісту еритроцитів (за вагою) і близько 35 % загального їх вмісту (враховуючи воду). Гемоглобін має здатність прив'язати до себе 1.34 мл O2 на грам речовини, що збільшує загальну ємність кисню в крові у 70 разів, порівнюючи з просто розчиненим у крові киснем. Молекула гемоглобіну ссавців може прив'язати (перенести) до 4 молекул кисню. Гемоглобін також залучений до транспорту інших газів: він переносить частину вуглекислого газу (близько 20–25 % загальної кількості) у вигляді карбогемоглобіна, у якому CO2 прив'язується до . Молекула також переносить важливу регуляторну молекулу оксид азоту(II) (NO), зв'язану з тіоловою групою білка глобіну, вивільняючи його одночасно з киснем. Гемоглобін також був знайдений за межами еритроцитів і їх прогеніторних ліній. Серед інших клітин, які містять гемоглобін, є у чорній речовині, макрофаги, клітини альвеол, легені, пігментний епітелій сітківки, гепатоцити, клітини ниркового , клітини ендометрія, клітини шийки матки і вагінальні епітеліальні клітини. У цих тканинах гемоглобін виконує не киснево-транспортну функцію, а функції антиоксиданта і регулятора . Надмірний вміст глюкози в крові може приєднатися до гемоглобіну і підвищити рівень гемоглобіну A1c. Гемоглобін і гемоглобіноподібні молекули також наявні в багатьох безхребетних, грибів і рослин. У цих організмів гемоглобін може переносити кисень або транспортувати та регулювати інші малі молекули та іони, такі як вуглекислий газ, оксид азоту, сірководень та сульфід. Варіант молекули, який називається , використовується для видалення кисню з анаеробних систем, таких як азот-фіксуючі клубні бобових рослин, щоб кисень не отруїв (деактивував) систему. Гемоглобінемія — це медичний стан, при якому спостерігається надлишок гемоглобіну в плазмі крові. Це є ефектом внутрішньосудинного гемолізу, при якому гемоглобін відділяється від еритроцитів, форма анемії. ( 영화에 대해서는 헤모글로빈 (영화) 문서를 참고하십시오.) 헤모글로빈(hemoglobin, haemoglobin) 또는 혈색소(血色素)는 적혈구에서 철을 포함하는 붉은 색 단백질로, 산소를 운반하는 역할을 한다. 헤모글로빈은 산소 분압이 높은 폐에서는 산소와 잘 결합하고, 산소 분압이 낮은 체내에서는 결합하던 산소를 유리하는 성질이 있다. 분자식은 C3032H4816O872N780S8Fe4 이다. 분자식에서 설명한 것처럼 철 원자가 4개 포함되어 있기 때문에 철이 부족하면 헤모글로빈이 완전하게 기능할 수 없어 빈혈(anemia)이 일어나게 된다. 철을 포함한 포르피린 고리와 단백질의 일종(글로빈)을 포함한 헴(heme)이라는 구조 4개가 모여 이루어진다. 철원자 1개에 대해 한 분자씩의 산소가 결합하므로, 헤모글로빈 한 분자에는 산소 4분자가 결합한다. 생체 내에서 산소를 운반하는 일을 한다. 산소가 풍부한 폐나 아가미에서는 산소와 결합하고, 산소가 희박한 조직에 이르면 산소를 떼어낸다. 산소의 방출은 pH가 낮아질수록 촉진되므로, 이산화 탄소가 많고 pH가 낮은 말초조직에서는 산소를 쉽게 떼어낼 수 있다. 이산화탄소가 혈장 속에 녹아 폐로 운반되어 폐호흡으로 체외에 방출되면 pH는 다시 원상태로 돌아가고 헤모글로빈은 다시 산소와 결합한다. Hemoglobin (haemoglobin BrE) (from the Greek word αἷμα, haîma 'blood' + Latin globus 'ball, sphere' + -in) (/ˌhiːməˈɡloʊbɪn, ˈhɛmoʊˌ-/), abbreviated Hb or Hgb, is the iron-containing oxygen-transport metalloprotein present in red blood cells (erythrocytes) of almost all vertebrates (the exception being the fish family Channichthyidae) as well as the tissues of some invertebrates. Hemoglobin in blood carries oxygen from the respiratory organs (e.g. lungs or gills) to the rest of the body (i.e. tissues). There it releases the oxygen to permit aerobic respiration to provide energy to power functions of an organism in the process called metabolism. A healthy individual human has 12 to 20 grams of hemoglobin in every 100 mL of blood. In mammals, the chromoprotein makes up about 96% of the red blood cells' dry content (by weight), and around 35% of the total content (including water). Hemoglobin has an oxygen-binding capacity of 1.34 mL O2 per gram, which increases the total blood oxygen capacity seventy-fold compared to dissolved oxygen in blood. The mammalian hemoglobin molecule can bind (carry) up to four oxygen molecules. Hemoglobin is involved in the transport of other gases: It carries some of the body's respiratory carbon dioxide (about 20–25% of the total) as carbaminohemoglobin, in which CO2 is bound to the heme protein. The molecule also carries the important regulatory molecule nitric oxide bound to a thiol group in the globin protein, releasing it at the same time as oxygen. Hemoglobin is also found outside red blood cells and their progenitor lines. Other cells that contain hemoglobin include the A9 dopaminergic neurons in the substantia nigra, macrophages, alveolar cells, lungs, retinal pigment epithelium, hepatocytes, mesangial cells in the kidney, endometrial cells, cervical cells and vaginal epithelial cells. In these tissues, hemoglobin has a non-oxygen-carrying function as an antioxidant and a regulator of iron metabolism. Excessive glucose in one's blood can attach to hemoglobin and raise the level of hemoglobin A1c. Hemoglobin and hemoglobin-like molecules are also found in many invertebrates, fungi, and plants. In these organisms, hemoglobins may carry oxygen, or they may act to transport and regulate other small molecules and ions such as carbon dioxide, nitric oxide, hydrogen sulfide and sulfide. A variant of the molecule, called leghemoglobin, is used to scavenge oxygen away from anaerobic systems, such as the nitrogen-fixing nodules of leguminous plants, lest the oxygen poison (deactivate) the system. Hemoglobinemia is a medical condition in which there is an excess of hemoglobin in the blood plasma. This is an effect of intravascular hemolysis, in which hemoglobin separates from red blood cells, a form of anemia. هيموغلوبين أو هيموجلوبين أو خضاب الدم أو اليحمور (بالإنجليزية: Haemoglobin)‏ هو بروتين محمول داخل خلايا الدم الحمراء ويحتوي على ذرات الحديد (Fe). يلتقط الأوكسجين في الرئتين ويسلّمه إلى الأنسجة للحفاظ على حياة الجسم. يتكون الهيموجلوبين من بروتينين متماثلين ملتصقين ببعضهما بعضا. يجب تواجد كِلا البروتينين ليستطيع الهيموجلوبين تحميل وإعطاء الأوكسجين لخلايا الجسم. أحد البروتينين يدعى ألفا، والآخر بيتا. قبل الولادة، لا يتم إنتاج بروتين بيتا. لكن يوجد بروتين آخر يحل مكانه يسمى غاما، وهو لا يوجد إلا في طور الجنين، ويعمل كبديل للبيتا حتى وقت الولادة. مثل جميع البروتينات، مخطّطات تصنيع الهيموجلوبين مخزنة داخل الـ الحمض النووي الريبوزي منقوص الأكسجين (المادة التي تكون الجينات). الإنسان لديه، في العادة، أربعة جينات للتحكم بتصنيع بروتين ألفا (سلسلة ألفا). بينما يتحكم جينان آخران في تصنيع سلسلة البيتا. (يوجد أيضا جينين إضافيين للتحكم بإنتاج سلسلة غاما لدى الجنين). يتم إنتاج سلسلة ألفا وبيتا بنفس الكمية، على الرغم من العدد المختلف للجينات. ترتبط سلاسل البروتين تلك بخلايا الدم الحمراء النامية، وتبقى معا طيلة حياة خلية الدم الحمراء. Hemoglobino estas la feroentena ruĝkolorigaĵo en la eritrocitoj de la vertebruloj. La hemoglobino konstruiĝas el kvar feroligaj hemoj kiel prosteta grupo kaj el kiel proteina parto. Hemoglobino ebligas la transporton de oksigeno (O2, kaptita de la pulmoj aŭ brankoj dum enspiro de vertebruloj), al histoĉeloj, liverante al ili energion por la bonfunkcio de la organismo (Vd metabolismo-n). Aliflanke hemoglobino ebligas ankaŭ la transporton de karbona dioksido (CO2), produktita de tiaj ĉeloj, kiu estas emisiita al aero per la pulmoj aŭ brankoj dum elspiro. Karakterizaĵoj de la hemoglobin-molekulo: * globetforma proteino kun ekstrema solviĝemo * afineco al oksigen-regula kun du formoj kiel- R (´relaxed´, oksigen-liga)- T (´tense´, karbondioksid-liga) * ĝi konstruiĝas el 4 hemoj kaj 4 globinoj * protekto de la 2-valora hem-fero kontraŭ la valorŝanĝo. La hemoglobinurio estas la ĉeesto de libera hemoglobino en la urino kiel konsekvenco de intravaskula hemolizo. ヘモグロビン(hemoglobin、Hb、血色素)とは、ヒトを含む全ての脊椎動物や一部のその他の動物の血液中に見られる赤血球の中に存在するタンパク質である。酸素分子と結合する性質を持ち、肺から全身へと酸素を運搬する役割を担っている。赤色素であるヘムを持っているため赤色を帯びている。 以下では、特にことわりのない限り、ヒトのヘモグロビンについて解説する。 La hemoglobina es una hemoproteína de la sangre, de masa molecular de 64 000 g/mol (64 kDa), de color rojo característico, que transporta el dioxígeno (comúnmente llamado oxígeno), O2, desde los órganos respiratorios hasta los tejidos, el dióxido de carbono, CO2, desde los tejidos hasta los pulmones que lo eliminan y también participa en la regulación de pH de la sangre, en vertebrados y algunos invertebrados. La hemoglobina es una proteína de estructura cuaternaria, que consta de cuatro subunidades. Esta proteína forma parte de la familia de las hemoproteínas, ya que posee 1 grupo hemo en cada subunidad.​ L'emoglobina (indicata con la sigla Hb, dall'inglese hemoglobin) è una proteina globulare con struttura quaternaria formata da quattro subunità. È solubile e di colore rosso (cromoproteina). È presente nei globuli rossi dei vertebrati (esclusi alcuni pesci antartici) per i quali svolge la funzione vitale di trasporto dell'ossigeno molecolare da un compartimento ad alta concentrazione di O2, il sangue arterioso, ai tessuti. Ognuna delle sue 4 catene polipeptidiche è legata covalentemente a un gruppo prostetico detto eme, costituito da una molecola di protoporfirina IX (che rappresenta la componente organica) coordinante uno ione ferro Fe2+ (rappresentante la componente inorganica) che sporge leggermente dal piano della molecola. Laddove la protoporfirina IX incontri lo ione ferroso, legandolo, si va a formare la cosiddetta “ferroprotoporfirina” (che altro non è che il gruppo “eme” per come lo troviamo all’interno della proteina). Lo spazio che racchiude lo ione ferroso viene anche chiamato “spazio tetradentato” per la sua forma caratteristica. L'emoglobina è inoltre una proteina allosterica. Viene sintetizzata inizialmente a livello dei proeritroblasti policromatofili (precursori dei globuli rossi), rimanendo poi in alte concentrazioni all'interno dell'eritrocita maturo (che ha perso il nucleo). Le alterazioni di origine genetica della struttura primaria della molecola, che ne alterano la funzione, o della sua espressione, che ne alterano la quantità in circolo, vanno sotto il nome di emoglobinopatie (esempi sono l'anemia falciforme e la talassemia). Is éard is haemaglóibin ann ná próitéin ina bhfuil an haem-mhóilín, ina bhfuil adamh iarainn lárnach, a iompraíonn ocsaigin sa bhfuil. Tá dhá roinn sa bhfuil agus an toirt chéanna iontu: na cealla bána is dearga (na heiritricítí), agus an fuilphlasma. Sna heiritricítí atá an haemaglóibin lonnaithe. I dtimthriall amháin d'imshruthú na fola, agus an fhuil ag rith trí na ribeadáin fola sna scamhóga, idirleathann an ocsaigin isteach inti ó na hailbheolais, agus tagann dath dearg ar an bhfuil athnuaite seo. Sa timthriall eile den imshruthú, nuair a ritheann an fhuil trí na ribeadáin fola i bhfíocháin eile na colainne, idirleathann an ocsaigin amach as an bhfuil is idirleathann dé-ocsaíd charbóin isteach inti, agus tagann dath gorm dorcha uirthi. Tá galair ghéiniteacha ann a chuireann isteach ar fheidhmiú na haemaglóibine. Buaileann anaemacht chorráncheallach daoine gorma amháin. Is amhlaidh a bhíonn cuid de na móilíní haemaglóibine máchaileach ó bhreith, ionas go n-athchumann na heiritricítí ina gcorráin. Calcann na cealla athchumtha seo fuileadáin bheaga, rud a choimeádann ocsaigin ó fhíocháin, á milleadh. Mar thoradh, is annamh a mhaireann an t-ainniseoir thar 20 bliain d'aois. Tá galar géiniteach eile cosúil léi a bhuaileann daoine ó imeall na Meánmhara, anaemacht Cooley. Sa ghalar seo, bíonn cuid den haemaglóibin máchaileach ar shlí go dtiteann na heiritricítí as a chéile, agus milleann sé seo fíocháin, ceal ocsaigine. Hemoglobin, ofta förkortat Hb, ibland Hgb, är ett protein som finns i röda blodkroppar hos människan och många djur. Hemoglobinet står för syrgastransporten i blodet. I äldre litteratur stavas det ibland hämoglobin. Hemoglobinet transporterar syrgas från lungorna ut till kroppens övriga vävnader, exempelvis musklerna och hjärnan. Där lämnar hemoglobinet sitt syre och plockar upp avfallsprodukten koldioxid för att frakta den tillbaka till lungorna, där den lämnar kroppen. Namnets hem kommer från hemoglobinets järninnehållande hemgrupp, som binder syrgasmolekylen och ger blodet dess röda färg, och globin syftar på själva proteinet som liksom övriga proteiner i blodet är globulärt, det vill säga mer eller mindre runt till formen. Halten av hemoglobin i blodet kan ses som ett mått på blodets förmåga till syrgastransport, och kallas blodvärde. Η αιμοσφαιρίνη είναι πρωτεΐνη του αίματος η οποία προσδένει οξυγόνο. Είναι σφαιρική και αποτελείται από τέσσερις πολυπεπτιδικές αλυσίδες ανά δύο όμοιες και τέσσερα μόρια αίμης, τα οποία είναι ενωμένα ανά ένα σε κάθε αλυσίδα. L'hemoglobina (abreujada com a Hb o Hgb) és la proteïna que transporta l'oxigen i conté ferro. Es troba als glòbuls vermells dels vertebrats, i als teixits d'alguns invertebrats. En mamífers, la proteïna constitueix aproximadament un 97% del contingut sec del glòbul vermell, i al voltant d'un 35% del contingut total (incloent-hi aigua). L'hemoglobina transporta oxigen des dels pulmons o brànquies fins a la resta del cos (i.e. els teixits) on allibera l'oxigen per a l'ús de les cèl·lules. També té més varietat de funcions transport de gas i modulació que varien d'espècie a espècie, i són bastant diversos en alguns invertebrats. Per exemple, l'hemoglobina transporta CO₂ de tornada des dels teixits fins als pulmons. L'hemoglobina té una capacitat d'unió a l'oxigen d'entre 1.36 i 1.37 ml O₂ per gram d'hemoglobina, que augmenta la capacitat de plegament d'oxigen total en sang setanta vegades. L'hemoglobina es troba als eritròcits incloent-hi les neurones d'A9 dopaminèrgic a la substància negra, macròfags, cèl·lules alveolars, i cèl·lules mesangials del ronyó. En aquests teixits, no té la funció de transportador d'oxigen, sinó que actua com a antioxidant i regulador del metabolisme del ferro. Hemoglobin adalah (protein yang mengandung zat besi) di dalam sel darah merah yang berfungsi sebagai pengangkut oksigen dari paru-paru ke seluruh tubuh, pada mamalia dan hewan lainnya. Hemoglobin juga pengusung karbon dioksida kembali menuju paru-paru untuk dihembuskan keluar tubuh. Molekul hemoglobin terdiri dari , , dan empat gugus heme, suatu molekul organik dengan satu atom besi. Mutasi pada gen protein hemoglobin mengakibatkan suatu golongan penyakit menurun yang disebut , di antaranya yang paling sering ditemui adalah anemia sel sabit dan talasemia. Гемоглоби́н (от др.-греч. αἷμα «кровь» + лат. globus «шар») (Hb или Hgb) — сложный железосодержащий белок животных, обладающих кровообращением, способный обратимо связываться с кислородом, обеспечивая его перенос в ткани. У позвоночных животных содержится в эритроцитах, у большинства беспозвоночных растворён в плазме крови (эритрокруорин) и может присутствовать в других тканях. Молекулярная масса гемоглобина человека — около 66,8 кДа. Молекула гемоглобина может нести до четырёх молекул кислорода. Один грамм гемоглобина может переносить до 1,34 мл кислорода. Hemoglobina (gr. αἷμα haîma "krew", łac. globus "kula"), oznaczana też skrótami Hb lub HGB – czerwony barwnik krwi, białko zawarte w erytrocytach, którego zasadniczą funkcją jest transportowanie tlenu – przyłączanie go w płucach i uwalnianie w tkankach. Mutacje genu hemoglobiny prowadzą do chorób dziedzicznych: anemii sierpowatej, talasemii lub rzadkich chorób zwanych hemoglobinopatiami. L'hémoglobine, couramment symbolisée Hb, parfois Hgb, est un pigment respiratoire (de la famille moléculaire des métalloprotéines, ici contenant du fer) présent essentiellement dans le sang des vertébrés, au sein de leurs globules rouges, ainsi que dans les tissus de certains invertébrés. Elle a pour fonction de transporter l'oxygène O2 depuis l'appareil respiratoire (poumons, branchies) vers le reste de l'organisme. La quantité d'hémoglobine est un paramètre mesuré lors d'un hémogramme. Hämoglobin (von altgriechisch αἷμα haíma, „Blut“, und lateinisch globus, „Klumpen, Ballen“), Abkürzung Hb, ist der eisenhaltige Proteinkomplex, der als Blutfarbstoff in den roten Blutkörperchen von Wirbeltieren enthalten ist, Sauerstoff bindet und diesen so im Blutkreislauf transportiert. Das Hämoglobin von Säugetieren ist ein Tetramer, es besteht aus vier Globinen als Untereinheiten. Beim erwachsenen Menschen sind dies je zwei Hb α und Hb β im Hämoglobin A (Hb A0), der häufigsten Form. Die vier den Komplex bildenden Proteine sind Aminosäureketten (α-Kette 141 AS; β-Kette 146 AS) in der für Globine typischen Faltung mit jeweils einer Tasche, in der ein Eisen-II-Komplex, das Häm, gebunden ist. Dessen Eisenion vermag ein Sauerstoffmolekül zu binden. Dabei ändert sich die Farbe des Häms von dunkel- zu hellrot. Die Bindungsstärke hängt empfindlich von der Konformation der Proteinumgebung des Häms ab. Wechselwirkungen zwischen den vier Globinen begünstigen die beiden extremen Zustände, in denen der Gesamtkomplex entweder mit vier Molekülen Sauerstoff gesättigt ist (in der Lunge bzw. den Kiemen) oder allen Sauerstoff abgegeben hat. Wechselwirkungen mit anderen Molekülen unterstützen die Beladung wie die Entladung. Zum Vorkommen von Hämoglobin und ähnlicher Globine im Tierreich siehe Sauerstofftransporter. Hemoglobine (Hb) is een gespecialiseerd eiwit dat het transport van zuurstof (O2) en koolstofdioxide (CO2) door het bloed van veel dieren verzorgt. Rode bloedcellen zijn voor 1/3 deel gevuld met hemoglobine. IJzer in het hemoglobine geeft bloed zijn rode kleur. De verbinding van zuurstof en hemoglobine (oxyhemoglobine) is lichtrood. In elke rode bloedcel bevinden zich circa 270 miljoen hemoglobinemoleculen (elke hemoglobinemolecuul kan maximaal 4 zuurstof (O2) of 4 koolstofdioxide (CO2) moleculen binden). Dit is ongeveer 34% van de inhoud van een normale rode bloedcel. Elke dag wordt 1% van de hemoglobine vernieuwd. Een volwassene heeft 600–800 gram hemoglobine, dat ongeveer 2,5 gram ijzer bevat (ca. 0,3%). 血红蛋白(Hemoglobin,縮寫 Hb、Hgb)又稱血红素,俗稱血色素,是高等生物体内红色含铁的携氧结合蛋白。血红蛋白的结构为异源四聚体,由2对珠蛋白组成,每个珠蛋白结合1个血基質。 哺乳动物的一个血红蛋白分子,可以结合最多四个氧分子。可以用平均細胞血紅蛋白濃度測出濃度。 Hemoglobina odolaren heteroproteina da, ugaztun eta beste ornodun batzuen globulu gorrietan dagoena. Bere eginkizun nagusia oxigenoaren garraioa da, arnas aparatutik gorputzeko ehunetara. Pigmentu gorria da, eta odolari gorri kolorea ematen dio. Bere pisu molekularra 64.000 Daltonekoa da. Hemoglobina, heteroproteina guztien antzera, talde proteikoz (proteinaz) eta talde prostetikoz (molekula ez-proteikoz) osatuta dago. Hemoglobinaren talde prostetikoa eraztun tetrapirrolikoa da, erdian burdin atomoa duena (ikusi irudia). Talde prostetikoari hemo taldea deritzo. Lau kate polipeptidikoek (bi α eta bi β) osatzen dute hemoglobina molekula, kate bakoitzak hemo talde bat duelarik. Oxigenoa hemo taldearen burdin atomoari lotzen zaio; hortaz, hemoglobina bakoitzak lau molekula oxigeno garraia dezake: Hb + 4O2 -> Hb(O2)4 Globulu gorriak hiltzen direnean barruko hemoglobina askatzen da, eta ehunetan dauden makrofagoek hemoglobina hori hartzen dute, bilirrubinan eraldatuz. Oxigenoa ez ezik, hemoglobinak karbono dioxidoa ere garraiatzen du. Oxigenoa biriketan lotu eta odolean zehar zeluletara garraiatzen duen bitartean, karbono dioxidoa metabolismoaren ondorioz gure zeluletan sortzen den produktua da eta biriketara garraiatzen du bertatik kanporatzeko. Oxigenoak odolean disolbatzeko duen gaitasun txikia dela eta, hemoglobina beharrezkoa da. Antzeko zerbait gertatzen da karbono dioxidoarekin, hau bikarbonato bezala garrraiatzen da odolean. Hemoglobina oxigenoari lotuta dagoenean izena hartzen du, karbono dioxidoari lotuta badago aldiz, . Karbono dioxidoa hemoglobinari lotzean, honek oxigenoa lotzeko duen gaitasuna jaitsi egiten du. Hau, Bohr efektua bezala ezagutzen da. Hemoglobinak oxigenoa hartzeko duen ahalmena asko murrizten da karbono monoxidoa (CO) aurrean, bi gasek lehia egiten dutelako hemoglobinari lotzeko (karbono monoxidoa hemoglobinari lotzen zaio oxigenoa lotzen zaion leku berean). Hala ere, hemoglobinak afinitate askoz handiagoa du karbono monoxidoarekiko (CO) oxigenoarekiko baino, 200 aldiz gehiago edo. Horrek esan nahi du CO eta O2 daudenean, hemoglobinak CO hartuko duela oxigenoaren ordez. Hori dela eta, CO oso gas toxikoa da, heriotza eragin dezakeena. Karbono monoxidoaren intoxikazioak asfixia eragiten du, biktimaren ehunek ez baitute oxigenoa jasotzen (oxigenoaren ordez CO eramaten baitu hemoglobinak). Karbono monoxidoarekin konbinatzen denean, gorri koloreko konposatu bat eratzen du hemoglobinak, izenekoa; horrek ematen die karbono monoxido intoxikazioaren ondorioz hildako biktimei duten kolore arrosa berezia. Era berean, hemoglobinak ere afinitatea du zianuroarekiko (CN), sufre monoxidoarekiko (SO) eta nitrogeno dioxidoarekiko (NO2). Substantzia horiek guztiak toxikoak dira, oxigenoa eta hemoglobinaren arteko lotura eragozten dutelako. Gorputzean hemoglobinaren maila normalak 12,5-18gr/dL-koak dira. Anemia dagoenean maila horiek jaisten dira. Bihotzeko hainbat gaitzek, aldiz, maila horiek igotzen dituzte.
dbp:cofactors
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dbp:formula
C2952 H 4664 O 832 N812 S8 Fe 4
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oxygen-transport
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Hemoglobin
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Structure of human hemoglobin. α and β subunits are in red and blue, respectively, and the iron-containing heme groups in green. From
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Chr. 11 p15.5 Chr. 16 p13.3
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heterotetramer, 2
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