Accession Number : AD0702263

Title :   STUDIES ON POLYMERIC STRUCTURE OF HEMOGLOBIN AND ITS RELATION TO THE FUNCTION.

Descriptive Note : Rept. no. 4 (Final), 4 Oct 68-3 Oct 69,

Corporate Author : NARA MEDICAL COLL KASHIHARA CITY (JAPAN) DEPT OF PHYSIOLOGY (2ND)

Personal Author(s) : Enoki,Yasunori

Report Date : DEC 1969

Pagination or Media Count : 28

Abstract : A procedure was developed for obtaining the delta(A2) subunit in a physiologically active state. The isolated subunit was identified by starch gel electrophresis and tryptic peptide mapping. The number of the reactive SH group was estimated as two per chain. The oxygen equilibrium was characterized by an increased affinity toward oxygen, and absence of heme-heme interaction and the Bohr effect. The oxygen affinity was found to be lower than that of the beta(A) subunits. All these findings are essentially the same as those for other single subunit hemoglobins. Oxygenation properties of partially oxidized hemoglobin were examined. An increase in the oxygen affinity and a decrease in the heme-heme interaction were associated with the partial oxidation of hemoglobin (Darling-Roughton effect). Quantitative relationships between the former two changes and the latter were established. The oxidation, however, had no influence upon the normal Bohr effect. (Author)

Descriptors :   (*HEMOGLOBIN, *MOLECULAR STRUCTURE), (*POLYMERS, HEMOGLOBIN), BLOOD, ELECTROPHORESIS, CHROMATOGRAPHIC ANALYSIS, OXYGEN, EQUILIBRIUM(PHYSIOLOGY), JAPAN

Subject Categories : Biochemistry
      Anatomy and Physiology

Distribution Statement : APPROVED FOR PUBLIC RELEASE