The hemoglobin system of the primitive fish, Amia calva: isolation and functional characterization of the individual hemoglobin components.

Journal Article

Blood from the primitive holostean fish, the bowfin, Amia calva, contains 2 mo of ATP per mol of hemoglobin. The hemolysates contain at least five tetrameric hemoglobin components which differ in their oxygen affinities and their response to cofactors such as ATP. The binding of oxygen by each chromatographically isolated component, including a cathodal component, is influenced by pH and organic phosphates; there is no significant differentiation of function or structure as seen in trout and certain other fish hemolysates. Kinetic analyses of ligand binding indicate that the Bohr and Root effects of Amia calva hemoglobins are best explained by changes in both the "on" and "off" constants. At low pH, the increase in the "off" constant is smaller than for most other Root hemoglobins. The hemoglobin system of Amina calva is functionally undifferentiated and may be representative of the ancestral condition in teleosts.

Full Text

Duke Authors

Cited Authors

  • Weber, RE; Sullivan, B; Bonaventura, J; Bonaventura, C

Published Date

  • May 20, 1976

Published In

Volume / Issue

  • 434 / 1

Start / End Page

  • 18 - 31

PubMed ID

  • 938661

International Standard Serial Number (ISSN)

  • 0006-3002

Language

  • eng

Conference Location

  • Netherlands