Structural relatedness of mouse lactate dehydrogenase isozymes, A4(muscle), B4(heart), and C4(testis)
✍ Scribed by Shou-Mei T. Chang; Chi-Yu Lee; Steven S.-L. Li
- Publisher
- Springer
- Year
- 1979
- Tongue
- English
- Weight
- 729 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0006-2928
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✦ Synopsis
Three homotetrameric lactate dehydrogenase isozymes, LDH-M(A4), LDH-H(B4), and LDH-X(C4), from DBA/2J mice have been purified by affinity chromatography. The amino acid compositions of the subunits A, B, and C, based on a molecular weight of 36,000, have been determined. The compositional relatedness of these isozymes indicates that subunits A (muscle) and B (heart) are more closely related to each other than to subunit C (testis). Tryptic peptide maps and amino acid compositions of some active site peptides appear to confirm the compositional relatedness among these isozymes. The sequence of the loop region of mouse C subunit seems to be markedly different from all known A and B sequences, and the structural and functional implications are discussed.