A Comparison of Some Kinetic Properties of Soluble and Bound Lactate Dehydrogenase Isoenzymes at Different Temperatures
- 1 August 1976
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 67 (1), 87-94
- https://doi.org/10.1111/j.1432-1033.1976.tb10636.x
Abstract
A comparison was made of some kinetic properties of 3 chicken lactate dehydrogenase [LDH, EC 1.1.1.27] isoenzymes (1, 3 and 5) at 4, 16, 23 and 40.degree. C. Assays were performed with an enzyme concentration of 0.01 .mu.M at pH 6.0. Under the conditions of assay, LDH 3 and 5 bound to the particulate fraction of homogenized skeletal muscle and were evaluated in the soluble and particulate state. Binding of isoenzymes 3 and 5 to the cellular particulate fraction decreased V. This decrease was much greater for LDH 5 than 3. Values of V for LDH isoenzymes 1 and 3 did not follow a simple Arrhenius relationship; there was a rapid change in activity between 16 and 23.degree. C. The apparent Km (pyruvate) values of all isoenzymes (bound or soluble) increased with increasing temperature, changing 4 to 10-fold. The apparent Km for LDH 5 was greater than that for LDH 3, which in turn was greater than that for LDH 1.This publication has 43 references indexed in Scilit:
- TEMPERATURE DEPENDENCE OF THE MICHAELIS CONSTANT OF CHICKEN BREAST MUSCLE LACTATE DEHYDROGENASEJournal of Food Science, 1973
- SUBSTRATE INHIBITION OF CHICKEN MUSCLE LACTATE DEHYDROGENASE AS A FUNCTION OF TEMPERATUREJournal of Food Science, 1973
- Studies on the nature of the subcellular localization of lactate dehydrogenase and glyceraldehyde‐3‐phosphate dehydrogenase in chicken skeletal muscleJournal of Cellular Physiology, 1973
- MODIFICATION OF KINETIC PROPERTIES OF MUSCLE LACTATE DEHYDROGENASE BY SUBCELLULAR ASSOCIATIONS AND POSSIBLE ROLE IN THE CONTROL OF GLYCOLYSISJournal of Food Science, 1972
- MUSCLE CONTRACTION AND POSTMORTEM pH CHANGES IN PIG SKELETAL MUSCLEJournal of Food Science, 1970
- Conformational changes in rabbit muscle aldolase. Kinetic studiesBiochemistry, 1970
- Isoenzymes and Short-term Temperature Compensation in Poikilotherms: Activation of Lactate Dehydrogenase Isoenzymes by Temperature DecreasesNature, 1969
- Intracellular Distribution of the Different Forms of Lactic DehydrogenaseNature, 1966
- Lactate Dehydrogenase Isozymes: Substrate Inhibition in Various Human TissuesScience, 1965
- THE DISTRIBUTION OF LACTATE DEHYDROGENASE ISOZYMES IN HUMAN SKELETAL MUSCLE FIBERSJournal of Histochemistry & Cytochemistry, 1964