Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1976 Feb 1;153(2):165–172. doi: 10.1042/bj1530165

Properties of the testicular lactate dehydrogenase isoenzyme.

A Blanco, C Burgos, N M Gerez de Burgos, E E Montamat
PMCID: PMC1172559  PMID: 1275882

Abstract

1. Studies were carried out with pure lactate dehydrogenase isoenzymes C4 (LDH isoenzyme X), B4, (LDH isoenzyme 1) and A4 (LDH isoenzyme 5) isolated from mouse testis, heart and muscle tissue respectively; with LDH isoenzyme X purified from pigeon testes and with crude lysates of spermatozoa from man, bull and rabbit. 2. LDH isoenzyme X from all species showed greater ability than the other isoenzymes to catalyse the NAD+-linked interconversions of 2-oxobutanoate into 2-hydroxybutanoate and of 2-oxopentanoate into 2-hydroxypentanoate. 3. Mouse LDH isoenzyme X presented the broadest spectrum of substrate specificity. It exhibited very similar Km values for a variety of 2-oxo acids: 2-oxopropanoate (pyruvate), 2-oxobutanoate, 2-oxo-3-methylbutanoate, 2-oxopentanoate, 2-oxo-3-methylpentanoate, 2-oxo-4-methylpentanoate, 2-oxohexanoate and 2-oxo-3-phenylpropanoate (phenylpyruvate). The corresponding 2-hydroxy acids were also readily utilized in the reverse reaction. A strong inhibition by substrate and product was demonstrated for the direct reaction. 4. Intracellular distribution of LDH isoenzyme X was investigated in mouse testes. LDH isoenzyme X activity was located in the fraction of "heavy mitochondria" and in the soluble phase. 5. A possible functional role for LDH isoenzyme X is proposed: the redox couple-2-oxo acid-2-hydroxy acid could integrate a shuttle system transferring reducing equivalents from cytoplasm to mitochondria.

Full text

PDF
165

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. ALLEN J. M. Multiple forms of lactic dehydrogenase in tissues of the mouse: their specificity, cellular localization, and response to altered physiological conditions. Ann N Y Acad Sci. 1961 Nov 2;94:937–951. doi: 10.1111/j.1749-6632.1961.tb35586.x. [DOI] [PubMed] [Google Scholar]
  2. BLANCO A., ZINKHAM W. H., KUPCHYK L. GENETIC CONTROL AND ONTOGENY OF LACTATE DEHYDROGENASE IN PIGEON TESTS. J Exp Zool. 1964 Jul;156:137–152. doi: 10.1002/jez.1401560202. [DOI] [PubMed] [Google Scholar]
  3. Baccetti B., Pallini V., Burrini A. G. Localization and catalytic properties of lactate dehydrogenase in different sperm models. Exp Cell Res. 1975 Jan;90(1):183–190. doi: 10.1016/0014-4827(75)90372-9. [DOI] [PubMed] [Google Scholar]
  4. Battellino L. J., Blanco A. Catalytic properties of the lactate dehydrogenase isozyme "X" from mouse testis. J Exp Zool. 1970 Jun;174(2):173–186. doi: 10.1002/jez.1401740207. [DOI] [PubMed] [Google Scholar]
  5. Battellino L. J., Blanco A. Testicular lactate dehydrogenase isozyme. Nature of multiple forms in guinea pig. Biochim Biophys Acta. 1970 Aug 15;212(2):205–212. doi: 10.1016/0005-2744(70)90201-9. [DOI] [PubMed] [Google Scholar]
  6. Battellino L. J., Jaime F. R., Blanco A. Kinetic properties of rabbit testicular lactate dehydrogenase isozyme. J Biol Chem. 1968 Oct 10;243(19):5185–5192. [PubMed] [Google Scholar]
  7. Blanco A., Zinkham W. H. Lactate Dehydrogenases in Human Testes. Science. 1963 Feb 15;139(3555):601–602. doi: 10.1126/science.139.3555.601. [DOI] [PubMed] [Google Scholar]
  8. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  9. Goldberg E. Amino acid composition and properties of crystalline lactate dehydrogenase X from mouse testes. J Biol Chem. 1972 Apr 10;247(7):2044–2048. [PubMed] [Google Scholar]
  10. Halestrap A. P. The mitochondrial pyruvate carrier. Kinetics and specificity for substrates and inhibitors. Biochem J. 1975 Apr;148(1):85–96. doi: 10.1042/bj1480085. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hawtrey C. O., Goldberg E. Some kinetic aspects of sperm specific lactate dehydrogenase in mice. J Exp Zool. 1970 Aug;174(4):451–461. doi: 10.1002/jez.1401740408. [DOI] [PubMed] [Google Scholar]
  12. Klingenberg M. Metabolite transport in mitochondria: an example for intracellular membrane function. Essays Biochem. 1970;6:119–159. [PubMed] [Google Scholar]
  13. Kolb E., Fleisher G. A., Larner J. Isolation and characterization of bovine lactate dehydrogenase X. Biochemistry. 1970 Oct 27;9(22):4372–4380. doi: 10.1021/bi00824a018. [DOI] [PubMed] [Google Scholar]
  14. Lancaster G., Mamer O. A., Scriver C. R. Branched-chain alpha-keto acids isolated as oxime derivatives: relationship to the corresponding hydroxy acids and amino acids in maple syrup urine disease. Metabolism. 1974 Mar;23(3):257–265. doi: 10.1016/0026-0495(74)90064-x. [DOI] [PubMed] [Google Scholar]
  15. Machado de Domenech E., Domenech C. E., Aoki A., Blanco A. Association of the testicular lactate dehydrogenase isozyme with a special type of mitochondria. Biol Reprod. 1972 Feb;6(1):136–147. doi: 10.1093/biolreprod/6.1.136. [DOI] [PubMed] [Google Scholar]
  16. Mowbray J. A mitochondrial monocarboxylate transporter in rat liver and heart and its possible function in cell control. Biochem J. 1975 Apr;148(1):41–47. doi: 10.1042/bj1480041. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. SALISBURY G. W., LODGE J. R. Metabolism of spermatozoa. Adv Enzymol Relat Subj Biochem. 1962;24:35–104. doi: 10.1002/9780470124888.ch2. [DOI] [PubMed] [Google Scholar]
  18. Schatz L., Segal H. L. Reduction of alpha-ketoglutarate by homogeneous lactic dehydrogenase X of testicular tissue. J Biol Chem. 1969 Aug 25;244(16):4393–4397. [PubMed] [Google Scholar]
  19. Wilkinson J. H., Withycombe W. A. Organ specificity and lactate-dehydrogenase activity. Some properties of human spermatozoal lactate dehydrogenase. Biochem J. 1965 Dec;97(3):663–668. doi: 10.1042/bj0970663. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Wong C., Yañez R., Brown D. M., Dickey A., Parks M. E., McKee R. W. Isolation and properties of lactate dehydrogenase isozyme X from Swiss mice. Arch Biochem Biophys. 1971 Oct;146(2):454–460. doi: 10.1016/0003-9861(71)90148-2. [DOI] [PubMed] [Google Scholar]
  21. ZINKHAM W. H., BLANCO A., CLOWRY L. J., Jr AN UNUSUAL ISOZYME OF LACTATE DEHYDROGENASE IN MATURE TESTES: LOCALIZATION, ONTOGENY, AND KINETIC PROPERTIES. Ann N Y Acad Sci. 1964 Dec 28;121:571–588. doi: 10.1111/j.1749-6632.1964.tb14227.x. [DOI] [PubMed] [Google Scholar]
  22. de Domenech E. M., Domenech C. E., Blanco A. Distribution of lactate dehydrogenase isozymes in subcellular fractions of rat tissues. Arch Biochem Biophys. 1970 Nov;141(1):147–154. doi: 10.1016/0003-9861(70)90117-7. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES