Zur Chemie des Blutfarbstoffes. (9. Mitteilung.) Über die Bindung zwischen Eiweiß und prosthetischer Gruppe im Hämoglobin.

Abstract

The experiments of Hill and Holden on the formation of hemoglobin from hemin and native globin were confirmed by means of gas analysis. The acid and unsaturated side chains of hemin are not concerned in the union of the globin because the union also results with dimethyl-mesohemin. Porphyrin was not bound by the globin. The linkage of the globin follows through the Fe atom of the prosthetic group and indeed through coordinatiye covalences. Native globin from the ox is a weak acid albumin, its isoelectric point is pH 6.9-7.0; coagulation point 47[degree]. Resynthesized hemoglobin is distinguished from native hemoglobin by a higher coagulation point, namely 63[degree], as compared with 47[degree].