Transamination with Purified Enzyme Preparations (transaminase)
نویسنده
چکیده
Braunstein and Kritzmann (1) have reported that with pigeon breast muscle any a-amino acid, with the possible exception of glycine, is active in transamination with either a-ketoglutaric or oxaloacetic acid. On the other hand, the author (2) found that transamination in pigeon breast muscle is limited to the following reactions. a (1) Z(+)-Glutamic acid + oxaloacetic acid e a-ketoglutaric acid b + I(-)-aspartic acid a (2) I(+)-Glutamic acid + pyruvic acid ti a-ketoglutaric acid b + Z(+)-alanine
منابع مشابه
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A wide variety of transaminase active on L-amino acids has been demonstrated in microorganisms (Feldman and Gunsalus, 1950; Fincham, 1951), mammalian tissues (Cammarata and Cohen, 1950; Rowsell, 1951), and plants (Wilson et al., 1954). Cohen (1939, 1940) did not find transaminase activity with any of several D-amino acids when he tested minced pigeon breast muscle or purified enzyme preparation...
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