Lactate dehydrogenases in spermatozoa: Subunit interactions in vitro

Erwin Goldberg*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

44 Scopus citations


The sperm-specific lactate dehydrogenase (LDH) isozyme from human, bovine, and murine sources has been dissociated, and its subunits have been recombined with subunits from the other forms of the enzyme. New LDH's are generated and have been characterized on the basis of substrate and coenzyme specificity. The properties of these new molecules are a reflection of their subunit composition, which, in turn, must determine either directly or indirectly the characteristics of the catalytic site(s) of the enzyme. The observations reported here demonstrate that the sperm-specific LDH contains polypeptide subunits which differ from those in LDH 1, 2, 3, 4, and 5.

Original languageEnglish (US)
Pages (from-to)134-141
Number of pages8
JournalArchives of biochemistry and biophysics
Issue number1
StatePublished - Jan 1965

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


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