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- Title
The Primary Structure and Functional Properties of the Hemoglobins of a Ground Squirrel (Spermophilus townsendii, Rodentia).
- Authors
KLEINSCHMIDT, Traute; BIEBER, Franz A.; NADLER, Charles F.; HOFFMANN, Robert S.; VIDA, Loyda N.; HONIG, George R.; BRAUNITZER, Gerhard
- Abstract
The hemoglobin of the ground squirrel Spermophilus townsendii consists of two components which are present in a ratio of ca. 2:1. The two hemoglobins have identical α-chains, but differ in their β-chains. We present the primary structures of the α- and the two β-globin chains. Following chain separation by chromatography on carboxymethyl-cellulose CM-52, the amino-acid sequences were established by automatic Edman degradation of the globin chains and the tryptic peptides, as well as of a peptide obtained by acid hydrolysis of the Asp-Pro bond of the β-chains. The two β-chains differ by only one amino-acid residue, Ala being present in the main and Asp in the minor component in position 58 (E 2). The comparison with human hemoglobin showed only 14 exchanges in the α-chains but 33 in the β-chains. Whereas no contact positions are affected in the α-chains, we found four such substitutions in the β-chains, including one heme contact, two α1/β1-contacts, and one α1/β2-contact. It seems however, that the substitution found in the β-chains has no effect on the oxygen affinity.
- Publication
Biological Chemistry, 1985, Vol 366, Issue 2, p971
- ISSN
1431-6730
- Publication type
Article