Comparative study of the structure of glyceraldehyde-3-phosphate dehydrogenase from bovine heart muscle

Comp Biochem Physiol B. 1986;85(4):811-8. doi: 10.1016/0305-0491(86)90180-x.

Abstract

Glyceraldehyde-3-phosphate dehydrogenase with a specific activity of 153 units/mg protein was isolated from bovine heart muscle. Its relative molecular mass was found to be 144,000. The tryptic peptide map and amino acid analysis were obtained. The N-terminal sequence was established as Val-Lys-Val-Gly-Val-Asn-Gly-... and C-terminal as ...-Ala-Ser-Lys-Glu. Fluorescence and optimal rotation dispersion measurements were performed. The data were compared with other glyceraldehyde-3-phosphate dehydrogenases.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Animals
  • Cattle
  • Glyceraldehyde-3-Phosphate Dehydrogenases / isolation & purification*
  • Glyceraldehyde-3-Phosphate Dehydrogenases / metabolism
  • Humans
  • Molecular Weight
  • Myocardium / enzymology*
  • Peptide Mapping
  • Protein Conformation
  • Species Specificity
  • Trypsin

Substances

  • Amino Acids
  • Glyceraldehyde-3-Phosphate Dehydrogenases
  • Trypsin