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Glycolytic, Pentose‐Phosphate Shunt and Transaminase Enzymes in Gastrocnemius Muscle, Liver, Heart, and Brain of Two Mouse Mutants, 129 J‐dy and A2G‐adr, with Abnormal Muscle Function
Author(s) -
Soothill Peter W.,
Kouseibati Farid,
Watts Rosemary L.,
Watts David C.
Publication year - 1981
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1981.tb00484.x
Subject(s) - pentose phosphate pathway , biology , medicine , endocrinology , mutant , glutamate dehydrogenase , biochemistry , dehydrogenase , glycolysis , aldolase a , enzyme , metabolism , glutamate receptor , receptor , gene
Aldolase and phosphoglycerate kinase activity were markedly reduced in muscle from two mouse mutants, 129 J‐dy and A2G‐adr, with abnormal muscle development. The pentose‐phosphate shunt enzymes, glucose‐6‐phosphate dehydrogenase and 6‐phosphogluconate dehydrogenase, were both greatly increased in the gastrocnemius of 129 J‐dy mice, but only the former was slightly increased in A2G‐adr muscle. Alanine and aspartate aminotransferase activities were normal or low in 129 J‐dy muscle but increased to approximately 200% in A2G‐adr muscle. Liver from 129 J‐dy mice showed increased activity of glucose‐6‐phosphate dehydrogenase. These findings are compatible with the well‐recognised lipid involvement in the 129 J‐dy mutant but indicate that an abnormality of amino acid metabolism in relation to energy supply is probably more important in the A2G‐adr mutant.