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Structural and functional comparison of trematode haemoglobins

Published online by Cambridge University Press:  05 June 2009

K.A. Rashid ,
M. Haque  and
A.H. Siddiqi
K.A. Rashid
Affiliation:
Section of Parasitology, Department of Zoology, Aligarh Muslim University, Aligarh 202 002, U.P., India
M. Haque
Affiliation:
Section of Parasitology, Department of Zoology, Aligarh Muslim University, Aligarh 202 002, U.P., India
A.H. Siddiqi
Affiliation:
Section of Parasitology, Department of Zoology, Aligarh Muslim University, Aligarh 202 002, U.P., India
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Abstract

Haemoglobins from three different species of trematodes (Gastrothylax crumenifer, Paramphistomum epiclitum and Isoparorchis hypselobagri) and their respective hosts were digested with papain. Peptides so produced were separated on 10–15% SDS-PAGGE. The probability of coincidence of the peptides was analysed statistically. Oxygen affinity curves of trematode haemoglobins were found to be a rectangular hyperbolic. The Hill coefficient values of all the trematode haemoglobins were found to be 1. The P50 values, at 25°C in 0.2M phosphate buffer pH 7.4, ranged from 0.8 to 1.6 mmHg.

Information

Type
Research Papers
Information
Journal of Helminthology , Volume 69 , Issue 1 , March 1995 , pp. 65 - 68
Copyright
Copyright © Cambridge University Press 1995

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