Structural and functional comparison of trematode haemoglobins.

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 degrees C in 0.2M phosphate buffer pH 7.4, ranged from 0.8 to 1.6 mmHg.