PMID: 639826Apr 1, 1978Paper

Phosphoglycerate kinase B from ram testis. Purification, characterisation and comparison with the muscle isoenzyme

European Journal of Biochemistry
A A Stewart, R K Scopes

Abstract

1. The testis-specific isoenzyme of phosphoglycerate kinase (phosphoglycerate kinase B) has been isolated from ram testes using a procedure which separates it from 'normal' phosphoglycerate kinase which is also present in testis tissue. The purification procedure is described. 2. The best preparations had no detectable impurity on electrophoresis, and had specific activities comparable with the same enzyme from other sources. 3. Kinetic studies indicated that the two isoenzymes have identical properties, within experimental error, for substrate affinity (for MgATP, 3-phosphoglycerate and MgADP), energy of activation and thermal denaturation. 4. The molecular weights of both isoenzymes were not distinguishably different from those previously reported, as measured by polyacrylamide/dodecylsulphate electrophoresis. The amino acid compositions showed only slight differences, and tryptic peptide maps showed that there was close homology of sequence. Starch gel electrophoresis at pH 6.5 indicates that the B isoenzyme has 1--2 more positive charges than the A. 5. Phosphoglycerate kinase A isolated from sheep muscle was shown, within experimental error, to be identical to the phosphoglycerate kinase A isolated from testis. 6. The resul...Continue Reading

References

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Citations

Nov 1, 1983·The Journal of Experimental Zoology·J L Vandeberg
Nov 4, 2020·International Journal of Molecular Sciences·Melissa Carvajal-SernaAdriana Casao
Jul 26, 1982·Biochimica Et Biophysica Acta·L S Hiremath, M Rothstein

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