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A MODEL SYSTEM FOR STUDYING CHICKEN LACTATE DEHYDROGENASE‐5 IN THE PARTICULATE PHASE
Author(s) -
HIRWAY SUMESH C.,
HULTIN HERBERT O.
Publication year - 1977
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1977.tb14451.x
Subject(s) - lactate dehydrogenase , dehydrogenase , chemistry , carboxymethyl cellulose , enzyme , biochemistry , glyceraldehyde 3 phosphate dehydrogenase , nicotinamide adenine dinucleotide , nad+ kinase , chromatography , sodium , organic chemistry
The effect of the interaction of chicken lactate dehydrogenase isoenzyme 5 with carboxymethyl cellulose (CMC) on some kinetic properties was studied. The effect of pH and the concentration of salt, reduced nicotinamide adenine dinucleotide (NADH), and glyceraldehyde‐3‐phosphate dehydrogenase on binding of chicken LDH‐5 to CMC was determined and found to be qualitatively similar to that observed earlier for the interaction of LDH with the particulate fraction of muscle but showed quantitative differences. Modifications of the catalytic properties of LDH on binding to CMC and muscle particles may be due to interactions between the enzyme and the insoluble support or to a change in the microenvironment of the enzyme.