含氧和脱氧血红蛋白之间的差异

Key Difference – Oxygenated vs Deoxygenated Hemoglobin

Hemoglobin is aprotein在发现红细胞，将氧气从肺部和器官以及二氧化碳从身体组织和器官带到肺部。血红蛋白有两种状态：氧化和脱氧血红蛋白。氧化和脱氧血红蛋白之间的关键区别在于oxygenated hemoglobin is the state of hemoglobin bound with four oxygen molecules while the deoxygenated hemoglobin is the unbound state of hemoglobin with oxygen.Oxygenated hemoglobin is bright red in colour while deoxygenated hemoglobin dark red in colour.

内容
1.Overview and Key Difference
2.What is Hemoglobin
3.What is Oxygenated Hemoglobin
4。什么是脱氧血红蛋白
4。并排比较 - 氧化与脱氧血红蛋白
5。总和mary

什么是血红蛋白？

血红蛋白（Hb）是红细胞中存在的复杂蛋白质分子，它为红细胞（圆形中心圆形）提供了典型的形状。HB的关键作用包括将氧气从肺部运输到人体组织，将其与二氧化碳交换，并将二氧化碳从身体组织中取出到肺部，并与氧气交换。血红蛋白分子包含四个多肽chains (protein subunits) and four heme groups as shown in figure 01. Four polypeptide chains represent two alpha球蛋白链条和两个β球蛋白链。Heme是血红蛋白分子中重要的卟啉化合物，其内部嵌入了中央铁原子。血红蛋白分子的每个多肽链都包含血红素基和铁原子。铁原子对于血液中氧气和二氧化碳的运输至关重要，它是红细胞红色的主要贡献者。血红蛋白也称为mettaloprotein由于其掺入铁原子。

Oxygen supply to tissues and organs is vital and essential. Cells obtain energy through有氧呼吸(oxidative phosphorylation) using oxygen as an electron acceptor. Production of energy is required for optimal cell metabolism and functions. Oxygen supply is facilitated by the hemoglobin proteins. Therefore hemoglobin is also known as oxygen carrying protein in the blood.

血液中低水平的血红蛋白称为贫血。贫血状况可能导致多种疾病。血液中血红蛋白浓度较低的原因不同。铁不足是主要原因，而过度节食，不健康的生活方式，一些疾病和癌症也是同样的原因。

血红蛋白分子具有四个与四个Fe相关的氧结合位点⁺²atoms. One molecule of hemoglobin can carry a maximum of four molecules of Oxygen. Hence, hemoglobin can be saturated or unsaturated with oxygen. Oxygen saturation is the percentage of oxygen binding sites of hemoglobin occupied by the oxygen. In other words, it measures the fraction of oxygen saturated hemoglobin relative to total hemoglobin. These two states of the hemoglobin are known as oxygenated and deoxygenated hemoglobin.

What is Oxygenated Hemoglobin?

When hemoglobin molecules are bound and saturated with oxygen molecules, the combination of hemoglobin with oxygen is known as oxygenated hemoglobin (催产蛋白). Oxygenated hemoglobin is formed during the physiological respiration (ventilation), when oxygen molecules bind with heme groups of the hemoglobin in red blood cells. Oxygenated hemoglobin production mainly happens in the pulmonary capillaries near to肺泡气体交换发生的肺（inhalation and exhalation). The affinity of oxygen binding to the hemoglobin is highly influenced by the pH. When the pH is high there is a high affinity of binding oxygen to hemoglobin but it decreases as the pH decreases. There is normally a high pH in lungs, and a low pH in muscles. Thus, this difference in pH conditions is useful for oxygen attachment, transportation and release. Since there is a high binding affinity near the lung, oxygen binds with hemoglobin and make oxyhemoglobin. When oxyhemoglobin reaches the muscle due to low pH, it dissolves and releases oxygen to the cells. Normal oxygen level in blood of humans are considered to be in the range of 95 – 100 %. Oxygenated blood is visible in bright red (crimson red) colour. When the hemoglobin is in the oxygenated form, it is also known as R state (Relaxed state) of the hemoglobin.

什么是脱氧血红蛋白？

Deoxygenated hemoglobin is the form of hemoglobin that is not bound to oxygen. Deoxygenated hemoglobin lacks oxygen. Hence this state called血红蛋白的T状态(紧张状态)。可以观察到脱氧血红蛋白when oxygenated hemoglobin releases oxygen and it is exchanged with carbon dioxide near the质膜of muscle cells那里的pH环境低。当血红蛋白对氧结合具有低亲和力时，它会递送氧并转化为脱氧血红蛋白。

What is the difference between Oxygenated and Deoxygenated Hemoglobin?

Oxygenated vs Deoxygenated Hemoglobin
Oxygenated hemoglobin is the combination of hemoglobin plus oxygen.	血红蛋白与氧的未结合形式称为脱氧血红蛋白。
氧分子状态
Oxygen molecules are bound to hemoglobin molecule.	氧分子与血红蛋白分子无结合。
颜色
含氧血红蛋白的颜色是鲜红色。	Deoxygenated hemoglobin is dark red in color.
血红蛋白的状态
这被称为r血红蛋白状态。	这被称为T (tense) state of Hemoglobin。
Formation
Oxygenated hemoglobin is formed when oxygen molecules bind with heme groups of the hemoglobin in red blood cells during the physiological respiration.	当氧气从氧化血红蛋白中释放并与肌肉细胞质膜附近的二氧化碳交换时，形成脱氧血红蛋白。

总和mary – Oxygenated and Deoxygenated Hemoglobin

血红蛋白是在红细胞中发现的一种重要蛋白质，能够从肺部携带氧气，并将二氧化碳从体组织带到肺部。由于氧的结合，血红蛋白的两种状态。这些是含氧血红蛋白和脱氧血红蛋白。当氧分子附着在Fe原子上时，会形成氧气血红蛋白。当氧分子从血红蛋白分子释放出来时，会形成脱氧的血红蛋白。这是氧化和脱氧血红蛋白之间的关键差异。氧气附着和释放主要受pH和氧气压力的影响。

Reference:
1. Thomas，Caroline和Andrew B. Lumb。“血红蛋白的生理学。”血红蛋白的生理学|BJA教育|牛津学术。牛津大学出版社，2012年5月15日。2017年2月20日。
2. Marengo-Rowe，Alain J.“人类血红蛋白的结构 - 功能关系。”会议记录（贝勒大学。医学中心）。贝勒卫生保健系统，2006年7月。2017年2月20日

Image Courtesy:
1. “1904 Hemoglobin” By OpenStax College – Anatomy & Physiology,Connexions Web site。(CC BY 3.0)viaCommons Wikimedia
2.“图39 04 01”CNX OpenStax–（CC由4.0）viaCommons Wikimedia
3. 2101 Blood Flow Through the Heart” By OpenStax College – Anatomy & Physiology,连接网站。(CC BY 3.0)viaCommons Wikimedia