On the spreading of different haemoglobins, muscle haemoglobins and cytochrome c
- 1 November 1939
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 33 (11) , 1743-1751
- https://doi.org/10.1042/bj0331743b
Abstract
Monolayers of horse (A), cow, dog, sheep (B), human, rabbit, cat and rat Hbs occupy an area at zero compression of 9,400 sq. cm. per mg. The time ts taken to reach this area varies with pH, salt conc. and sp. 2% urea does not affect ts; 25% greatly reduces ts. There is no difference between the final films of A and B on 25% urea, although in soln. A is split into molecules of half normal molecular wt., and B is not. Reduced Hb spreads more rapidly than HbO2; reduced cytochrome spreads more slowly than oxidised cytochrome. At the isoelectric point ts for Hbs is independent of total ion conc. Muscle Hb does not spread between pH 4 and 11 unless reduced.This publication has 4 references indexed in Scilit:
- Newer Biological Aspects of Protein ChemistryScience, 1937
- The occurrence of several kinds of hæmoglobin in human bloodThe Journal of Physiology, 1935
- AN APPARATUS FOR PRESSURE MEASUREMENTS OF SPREADING SUBSTANCESThe Journal of general physiology, 1935
- PROTEIN COAGULATION AND ITS REVERSALThe Journal of general physiology, 1930