Die Primärstruktur des Hämoglobins vom Goldfisch(Carassius auratus)

Publisher Website
Google Scholar
Abstract
The primary structures of the .alpha.- and .beta.-chains from goldfish Hb are given. The globin chains were separated by gel filtration after air-oxidation of globin. After chemical and enzymatic cleavage of the chains, the peptides were isolated by gel filtration and ion exchange chromatography on Dowex. The fish chains have 1 residue more than the human chains. The .alpha.-chain is acetylated at the amino-terminal residue and has no cysteines. Compared with the human chains there are 66 amino-acid differences in the .alpha.- and 72 in the .beta.-chains. The implication of these differences for the physiology of the Hb molecule of goldfish is discussed.

This publication has 29 references indexed in Scilit: