《生理学》 CHAPTER 5 RESPIRATION-2培训资料.ppt

特点：character 1.可逆性结合，非酶促过程，反应快，受PO2影响。 Reversible binding. Without enzyme. Fast. Effected by PO2. 2.O2与血红蛋白的亚铁离子结合，结合后亚铁离子的离子价不变，故称氧合，不是氧化。 O2 binds with Fe2+ of ferrohemoglobin . The ion value is permanent. So the process is called oxygenation but not oxidation. 3.血红蛋白的珠蛋白由两条α肽链和两条β肽链构成，每条肽链上结合一个含亚铁离子的血红素分子，每个亚铁离子结合一个O2分子。故每个血红蛋白分子可结合4个O2分子（HbO8）1gHb可结合1.34－1.39mlO2. Globin of ferrohemoglobin is made up of two αpeptide chains and two β peptide chains . There is a protoheme molecular on each peptide chain including a Fe2+. Each Fe2+ binds with an O2 . So each ferrohemoglobin can bind with four O2. （HbO8）1gHb can bind with 1.34－1.39mlO2. 4.血红蛋白两对α、β肽链与O2结合可互相促成结合或解离（释放）。 在肺部，PO2升高促结合； 在组织，PO2下降促释放。 Conjugation of peptide chains α、βof ferrohemoglobin and O2 can facilitate binding or dissociation(releasing). In lungs, increasing of PO2 promotes combination. In tissues, decreasing of PO2 promotes releasing. 5. Hb与O2的结合或解离曲线呈S型与Hb的变构效应有关 The binding or dissociation curves of Hb and O2 appear S form.This is related to the allosterism effect of Hb. Hb与O2结合－－盐键断裂，R型 Hb与O2解离－－盐键形成，T型 Hb binds with O2—salt bond breaks, R form Hb dissociates with O2—salt bond forms,T form T型对O2亲和力小。The affinity of T form to O2 is smaller. R型对O2亲和力大。 The affinity of R form to O2 is larger. 血红蛋白的异常形成 1.胎儿血红蛋白（HbF）是由两条γ链和α链结合组成，它对O2亲和力比HbA大。可能由于γ链不与2，3DPG相结合，不受2，3DPG影响的缘故。 2.镰状细胞贫血（HbS)两条β链第6位谷氨酸为缬氨酸所取代，使去氧Hb释放O2的能力下降，导致组织缺O2。 3.地中海贫血 。 我国常见β地贫。由于β链合成障碍HbA生成抑制，HbF代偿增多，O2解离曲线左移。 （二）氧解离曲线 oxygen dissociation curve 反映PO2与氧合Hb饱和度的关系的曲线。（图40-9） The curve reacts the relationship of PO2 and saturation of oxygenation Hb . (figure 40-9) 氧解离曲线 oxygen dissociation curve  特点：character 1.曲线上段：PO2 60－100mmHg. 坡度较平坦 Superior segment of curve: PO2 60－100mmHg. Slope is flat. 1）氧分压变化虽大但饱和度变异小－－即使外界或肺泡中PO2下降，但氧合饱和度依然可维持在较高水平。 Partial pressure of oxygen changes greatly. But saturation changes little—even PO2 of environment or alveoli descents, oxyg