Comparative study of the structure of glyceraldehyde-3-phosphate dehydrogenase from bovine heart muscle.
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.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000302:isolation & purification* / Q000378:metabolism; D006801:Humans; D008970:Molecular Weight; D009206:Myocardium / Q000201:enzymology*; D010449:Peptide Mapping; D011487:Protein Conformation; D013045:Species Specificity; D014357:Trypsin
D000596:Amino Acids; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D014357:Trypsin