Translations:Hämoglobin/1/en: Unterschied zwischen den Versionen

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Nachricht im Original (Hämoglobin)

Blutfarbstoff, der aus Globin als Proteinanteil und aus der eisenhaltigen prosthetischen Gruppe [https://de.wikipedia.org/wiki/H%C3%A4matine Hämatin] als aktives Zentrum der Sauerstoffbindung besteht. Jeder [[Erythrozyt]] besteht zu 90% aus Hämoglobin und damit enthält er ca. 250 Millionen Hämoglobin-Moleküle. Jedes Hämoglobinmolekül besteht aus vier Untereinheiten, die jede jeweils eine Häm-Gruppe enthalten. Im Zentrum der Häm-Gruppe ist ein Eisen-Ion gebunden. Dieses Eisen übt eine starke Anziehungskraft, sog. Affinität auf [[Sauerstoff]] aus, wodurch der Sauerstoff (bzw. jeweils ein Sauerstoffmolekül) an das Hämoglobin gebunden wird. Hämoglobin bindet den Sauerstoff (O<sub>2</sub>) unter dem hohen Partialdruck der Einatmungsluft in den Lungen und färbt sich hellrot (Oxyhämoglobin), unter dem niedrigen Partialdruck in den peripheren Geweben infolge des Sauerstoffverbrauchs gibt das Oxyhämoglobin den Sauerstoff ab und färbt sich dabei dunkelrot (reduziertes Hämoglobin). Daraus ergibt sich die unterschiedliche Färbung arteriellen und venösen Blutes, wie auch die rötliche Farbe gut durchbluteter Haut und die bläuliche bei schlechter Sauerstoffsättigung des arteriellen Blutes. Das Hämoglobin bildet nach dem Bikarbonat den wichtigsten Puffer des Blutes zur Konstanthaltung seines pH. Unter blauroter Verfärbung des Blutfarbstoffs verdrängt Kohlenmonoxyd (CO) infolge höherer Bindungsstärke den Sauerstoff vom Hämoglobin, wodurch dieser nicht mehr in das Gewebe transportiert werden kann. Die resultierende Gewebserstickung bedingt die Giftigkeit des Kohlenmonoxids.

ÜbersetzungA blood pigment consisting of globin as a protein component and the iron-containing prosthetic group [https://de.wikipedia.org/wiki/H%C3%A4matine Hematin] as the active centre of oxygen binding. Each [[Erythrozyt/en|erythrocyte]] consists of 90% haemoglobin and thus contains about 250 million haemoglobin molecules. Each haemoglobin molecule consists of four subunits, each containing a haem group. An iron ion is bound in the centre of the heme group. This iron exerts a strong attraction, so-called affinity, on [[Sauerstoff/en|oxygen]], whereby the oxygen (or one oxygen molecule in each case) is bound to the haemoglobin. Hemoglobin binds oxygen (O<sub>2</sub>) under the high partial pressure of inhalation air in the lungs and turns light red (oxyhaemoglobin), under the low partial pressure in peripheral tissues due to oxygen consumption, oxyhaemoglobin releases oxygen and turns dark red (reduced hemoglobin).

This results in the different colouring of arterial and venous blood, as well as the reddish colour of skin with good blood circulation and the bluish colour in case of poor oxygen saturation of the arterial blood. After bicarbonate, hemoglobin forms the most important buffer in the blood to keep its pH constant. Under a purple discoloration of the blood pigment, carbon monoxide (CO) displaces the oxygen from the haemoglobin as a result of higher binding strength, so that it can no longer be transported into the tissue. The resulting tissue nitrogenization causes the toxicity of carbon monoxide.

A blood pigment consisting of globin as a protein component and the iron-containing prosthetic group Hematin as the active centre of oxygen binding. Each erythrocyte consists of 90% haemoglobin and thus contains about 250 million haemoglobin molecules. Each haemoglobin molecule consists of four subunits, each containing a haem group. An iron ion is bound in the centre of the heme group. This iron exerts a strong attraction, so-called affinity, on oxygen, whereby the oxygen (or one oxygen molecule in each case) is bound to the haemoglobin. Hemoglobin binds oxygen (O₂) under the high partial pressure of inhalation air in the lungs and turns light red (oxyhaemoglobin), under the low partial pressure in peripheral tissues due to oxygen consumption, oxyhaemoglobin releases oxygen and turns dark red (reduced hemoglobin).

This results in the different colouring of arterial and venous blood, as well as the reddish colour of skin with good blood circulation and the bluish colour in case of poor oxygen saturation of the arterial blood. After bicarbonate, hemoglobin forms the most important buffer in the blood to keep its pH constant. Under a purple discoloration of the blood pigment, carbon monoxide (CO) displaces the oxygen from the haemoglobin as a result of higher binding strength, so that it can no longer be transported into the tissue. The resulting tissue nitrogenization causes the toxicity of carbon monoxide.

Version vom 22. Mai 2019, 00:25 Uhr (Quelltext anzeigen) 127.0.0.1 (Diskussion) (Fixed wikilinks.) ← Zum vorherigen Versionsunterschied		Aktuelle Version vom 7. Juli 2019, 15:08 Uhr (Quelltext anzeigen) Ischler (Diskussion \| Beiträge)
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−	A blood pigment consisting of globin as a protein component and the iron-containing prosthetic group [https://de.wikipedia.org/wiki/H%C3%A4matine Hematin] as the active centre of oxygen binding. Each [[Erythrozyt/en\|erythrocyte]] consists of 90% haemoglobin and thus contains about 250 million haemoglobin molecules. Each haemoglobin molecule consists of four subunits, each containing a haem group. An iron ion is bound in the centre of the heme group. This iron exerts a strong attraction, so-called affinity, on [[Sauerstoff/en\|oxygen]], whereby the oxygen (or one oxygen molecule in each case) is bound to the haemoglobin. Hemoglobin binds oxygen (O<sub>2</sub>) under the high partial pressure of inhalation air in the lungs and turns light red (oxyhaemoglobin), under the low partial pressure in peripheral tissues due to oxygen consumption, oxyhaemoglobin releases oxygen and turns dark red (reduced hemoglobin). This results in the different colouring of arterial and venous blood, as well as the reddish colour of skin with good blood circulation and the bluish colour in case of poor oxygen saturation of the arterial blood. After bicarbonate, hemoglobin forms the most important buffer in the blood to keep its pH constant. Under a purple discoloration of the blood pigment, carbon monoxide (CO) displaces the oxygen from the haemoglobin as a result of higher binding strength, so that it can no longer be transported into the tissue. The resulting tissue nitrogenization causes the toxicity of carbon monoxide.	+	A blood pigment consisting of globin as a protein component and the iron-containing prosthetic group [https://de.wikipedia.org/wiki/H%C3%A4matine Hematin] as the active centre of oxygen binding. Each [[Erythrozyt/en\|erythrocyte]] consists of 90% haemoglobin and thus contains about 250 million haemoglobin molecules. Each haemoglobin molecule consists of four subunits, each containing a haem group. An iron ion is bound in the centre of the heme group. This iron exerts a strong attraction, so-called affinity, on [[Sauerstoff/en\|oxygen]], whereby the oxygen (or one oxygen molecule in each case) is bound to the haemoglobin. Hemoglobin binds oxygen (O<sub>2</sub>) under the high partial pressure of inhalation air in the lungs and turns light red (oxyhaemoglobin), under the low partial pressure in peripheral tissues due to oxygen consumption, oxyhaemoglobin releases oxygen and turns dark red (reduced hemoglobin).
		+
		+	This results in the different colouring of arterial and venous blood, as well as the reddish colour of skin with good blood circulation and the bluish colour in case of poor oxygen saturation of the arterial blood. After bicarbonate, hemoglobin forms the most important buffer in the blood to keep its pH constant. Under a purple discoloration of the blood pigment, carbon monoxide (CO) displaces the oxygen from the haemoglobin as a result of higher binding strength, so that it can no longer be transported into the tissue. The resulting tissue nitrogenization causes the toxicity of carbon monoxide.