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Alkali denaturation of oxyhaemoglobins of some digenetic trematodes and their hosts

Published online by Cambridge University Press:  05 June 2009

S. Ashfaq Haider  and
Ather H. Siddiqi
S. Ashfaq Haider
Affiliation:
Section of Parasitology, Department of Zoology, Aligarh Muslim University, Aligarh 202 001, India
Ather H. Siddiqi
Affiliation:
Section of Parasitology, Department of Zoology, Aligarh Muslim University, Aligarh 202 001, India
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Abstract

Oxyhaemoglobins 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.

Type
Research Article
Information
Journal of Helminthology , Volume 51 , Issue 4 , December 1977 , pp. 373 - 378
Copyright
Copyright © Cambridge University Press 1977

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References

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