Molecular analysis of genetic mutation in electrophoretic variant of human lactate dehydrogenase-A(M) subunit

Biochem Int. 1992 Sep;27(6):1051-7.

Abstract

An electrophoretic variant of lactate dehydrogenase-A (M) subunit was discovered in a patient with multiple myeloma. DNA analysis of the variant allele revealed a nucleotide substitution (transition) of C to T at codon 314 (CGT-TGT), and this mutation resulted in the replacement of an arginine by a cysteine (R314C). This amino acid replacement affects the net charge of the subunit and makes the LDH-A variant have a faster electrophoretic mobility. The responsible missense mutation created a new restriction site, AGGCCT, which can be simply detected by endonuclease AatI digestion. In addition, four synonymous substitutions with no amino-acid replacements were found at codons 51, 119, 163 and 175 in the LDH-A gene from the patient.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aged
  • Amino Acid Sequence
  • Animals
  • Electrophoresis
  • Female
  • Humans
  • Isoenzymes
  • L-Lactate Dehydrogenase / blood
  • L-Lactate Dehydrogenase / genetics*
  • Molecular Sequence Data
  • Multiple Myeloma / enzymology
  • Mutation*
  • Polymerase Chain Reaction
  • Sequence Homology, Nucleic Acid

Substances

  • Isoenzymes
  • L-Lactate Dehydrogenase