一、变性血红蛋白:血红蛋白,是由 DFe 啶色素和蛋白质所形成的,前者叫做血红素,后者叫做珠蛋白,血红素能够很快的和氧结合,也容易将氧释放,这看血液内的氧分压大小如何,化学的反应式如左:Hb+O_2HbO_2正因为这样,组织内才能获到由肺所供给的氧。血红素这种对氧的可逆反应特性,据目下所知是由于二价铁 Fe~(++)即低铁的作用所致。因而在正常情况下,血红素中所含的铁是低铁。但低铁与血红素结合后怎样赋予它一种这样的特性呢,还是不大很清楚。据 Cecil 氏认为:“在正常情况下,低铁是和 bcc 咯环(Pyrrole rings)四个氮原子呈配价键(Coorqinate bonds)的结合,内中有两个配价键可以自由的与氧结合而形成含氧的血红蛋 First, the denatured hemoglobin: hemoglobin, DFe is formed by the pigment and protein, the former is called heme, which is called globin, heme oxygen can be quickly combined, but also easy to release oxygen, which see the blood Oxygen partial pressure how the size of the chemical reaction as the left: Hb + O_2HbO_2 Because of this, the tissue can be obtained by the oxygen supplied by the lungs. The reversible reaction of heme to oxygen, to the best of knowledge, is due to the action of ferrous iron Fe ~ (++), ie low iron. Under normal circumstances, therefore, iron contained in heme is low iron. However, the combination of low iron and hemoglobin how to give it such a feature it, or not very clear. According to Cecil, ”Under normal conditions, low iron is covalently bonded to the four nitrogen atoms of the bcc pyrrole rings. Two low valence bonds are free Oxygen combine to form oxygenated hemoglobin