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Purification of 2,3-bisphosphoglycerate synthase-phosphatase from pig skeletal muscle

Authors
Journal
Biochimica et Biophysica Acta (BBA) - General Subjects
0304-4165
Publisher
Elsevier
Publication Date
Volume
842
Issue
1
Identifiers
DOI: 10.1016/0304-4165(85)90293-4
Disciplines
  • Biology

Abstract

Abstract Two enzymes which possess 2,3-bisphosphoglycerate synthase, 2,3-bisphosphoglycerate phosphatase and phosphoglycerate mutase activities have been purified from pig skeletal muscle. One of the enzymes corresponds to type M phosphoglycerate mutase. The other enzyme shows properties similar to those of the 2,3-bisphosphoglycerate synthase-phosphatase present in mammalian erythrocytes. The erythrocyte and the muscle enzyme possess the same molecular (56 000) and subunit (27 000) weights. The synthase, phosphatase and mutase activity ratio is similar in both enzymes, and they are affected by the same inhibitor (glycerate3- P) and activators (glycolate 2- P), pyrophosphate, sulfite and bisulfite).

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