Abstract
Stopped-flow kinetics indicate that human and chicken heart-type4 lactate dehydrogenases (LDH) become inhibited as DPNH is oxidized in the presence of high concentrations of pyruvate. This inhibition is much less marked with the human and chicken muscle-type4 enzymes. The initial rates and the difference in inhibition between the two types of enzyme have made it possible to determine the amount of, as well as the ratio between, the two types of LDH that are present in a given sample by a single kinetic assay. The stopped-flow kinetic method has been used to analyze amounts of LDH isoenzyme in different tissues, as well as in serum.
Keywords: stopped-flow technique, serum enzymes, ternary complex
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- COHEN L., DJORDJEVICH J., ORMISTE V. SERUM LACTIC DEHYDROGENASE ISOZYME PATTERNS IN CARDIOVASCULAR AND OTHER DISEASES, WITH PARTICULAR REFERENCE TO ACUTE MYOCARDIAL INFARCTION. J Lab Clin Med. 1964 Sep;64:355–374. [PubMed] [Google Scholar]
- Cahn R. D., Zwilling E., Kaplan N. O., Levine L. Nature and Development of Lactic Dehydrogenases: The two major types of this enzyme form molecular hybrids which change in makeup during development. Science. 1962 Jun 15;136(3520):962–969. doi: 10.1126/science.136.3520.962. [DOI] [PubMed] [Google Scholar]
- DAWSON D. M., GOODFRIEND T. L., KAPLAN N. O. LACTIC DEHYDROGENASES: FUNCTIONS OF THE TWO TYPES RATES OF SYNTHESIS OF THE TWO MAJOR FORMS CAN BE CORRELATED WITH METABOLIC DIFFERENTIATION. Science. 1964 Feb 28;143(3609):929–933. doi: 10.1126/science.143.3609.929. [DOI] [PubMed] [Google Scholar]
- Everse J., Barnett R. E., Thorne C. J., Kaplan N. O. The formation of ternary complexes by diphosphopyridine nucleotide-dependent dehydrogenases. Arch Biochem Biophys. 1971 Apr;143(2):444–460. doi: 10.1016/0003-9861(71)90230-x. [DOI] [PubMed] [Google Scholar]
- Everse J., Berger R. L., Kaplan N. O. Physiological concentrations of lactate dehydrogenases and substrate inhibition. Science. 1970 Jun 5;168(3936):1236–1238. doi: 10.1126/science.168.3936.1236. [DOI] [PubMed] [Google Scholar]
- FONDY T. P., PESCE A., FREEDBERG I., STOLZENBACH F., KAPLAN N. O. THE COMPARATIVE ENZYMOLOGY OF LACTIC DEHYDROGENASES. II. PROPERTIES OF THE CRYSTALLINE HM3 HYBRID FROM CHICKEN MUSCLE AND OF H2M2 HYBRID AND H4 ENZYME FROM CHICKEN LIVER. Biochemistry. 1964 Apr;3:522–530. doi: 10.1021/bi00892a010. [DOI] [PubMed] [Google Scholar]
- FROMM H. DETERMINATION OF DISSOCIATION CONSTANTS OF COENZYMES AND ABORTIVE TERNARY COMPLEXES WITH RABBIT MUSCLE LACTATE DEHYDROGENASE FROM FLUORESCENCE MEASUREMENTS. J Biol Chem. 1963 Sep;238:2938–2944. [PubMed] [Google Scholar]
- Gutfreund H., Cantwell R., McMurray C. H., Criddle R. S., Hathaway G. The kinetics of the reversible inhibition of heart lactate dehydrogenase through the formation of the enzyme-oxidized nicotinamide-adenine dinucleotide-pyruvate compounds. Biochem J. 1968 Feb;106(3):683–687. doi: 10.1042/bj1060683. [DOI] [PMC free article] [PubMed] [Google Scholar]
- KAPLAN N. O. LACTATE DEHYDROGENASE--STRUCTURE AND FUNCTION. Brookhaven Symp Biol. 1964 Dec;17:131–153. [PubMed] [Google Scholar]
- Kaplan N. O., Everse J., Admiraal J. Significance of substrate inhibition of dehydrogenases. Ann N Y Acad Sci. 1968 Jun 14;151(1):400–412. doi: 10.1111/j.1749-6632.1968.tb11903.x. [DOI] [PubMed] [Google Scholar]
- Latner A. L., Siddiqui S. A., Skillen A. W. Pyruvate inhibition of lactate dehydrogenase activity in human tissue extracts. Science. 1966 Oct 28;154(3748):527–529. [PubMed] [Google Scholar]
- PESCE A., MCKAY R. H., STOLZENBACH F., CAHN R. D., KAPLAN N. O. THE COMPARATIVE ENZYMOLOGY OF LACTIC DEHYDROGENASES. I. PROPERTIES OF THE CRYSTALLINE BEEF AND CHICKEN ENZYMES. J Biol Chem. 1964 Jun;239:1753–1761. [PubMed] [Google Scholar]
- Pesce A., Fondy T. P., Stolzenbach F., Castillo F., Kaplan N. O. The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of vertebrates. J Biol Chem. 1967 May 10;242(9):2151–2167. [PubMed] [Google Scholar]
- VESELL E. S., BEARN A. G. Observations on the heterogeneity of malic and lactic dehydrogenase in human serum and red blood cells. J Clin Invest. 1958 May;37(5):672–677. doi: 10.1172/JCI103652. [DOI] [PMC free article] [PubMed] [Google Scholar]
- WIEME R. J., VAN MAERCKE Y. The fifth (electrophoretically slowest) serum lactic dehydrogenase as an index of liver injury. Ann N Y Acad Sci. 1961 Nov 2;94:898–911. doi: 10.1111/j.1749-6632.1961.tb35583.x. [DOI] [PubMed] [Google Scholar]
- WROBLEWSKI F., GREGORY K. F. Lactic dehydrogenase isozymes and their distribution in normal tissues and plasma and in disease states. Ann N Y Acad Sci. 1961 Nov 2;94:912–932. doi: 10.1111/j.1749-6632.1961.tb35584.x. [DOI] [PubMed] [Google Scholar]
- Wilkinson J. H. Clinical applications of isoenzymes. Clin Chem. 1970 Sep;16(9):733–739. [PubMed] [Google Scholar]




