Alkali denaturation of oxyhaemoglobins of some digenetic trematodes and their hosts

Author:

Haider S. Ashfaq,Siddiqi Ather H.

Abstract

ABSTRACTOxyhaemoglobins of six digenetic trematodes,—Srivastavaia indica, Gastrothylax crumenifer, Gigantocotyle explanatum, Fasciolopsis buski, Gastrodiscoides hominis, Isoparorchis hypselobagri, and of their 3 vertebrate hosts, Bubalus, bubalis, Sus scrofa, Wallago attu, were subjected to alkali denaturation at a pH of 12·4. All oxyhaemoglobins from trematodes and their hosts differ from each other in the rate and extent of alkali denaturation which may be explained due to variations in the amino acid sequences of a particular haem protein in addition to other factors.

Publisher

Cambridge University Press (CUP)

Subject

Animal Science and Zoology,General Medicine,Parasitology

Reference5 articles.

1. Protein-protein interaction among hemoglobin subunits

2. Chemical and physiological properties of the larval and the adult haemoglobins in rainbow trout, Salmo gairderii.;Iuchi;Comparative Biochemistry and Physiology,1973

3. Mechanism of denaturation of haemoglobin by alkali

4. Spectrophotometric analysis of haemoglobins of some digenetic trematodes and their hosts

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