1887

Abstract

Tyrosine aminotransferase, induced in by -tyrosine, was isolated from the culture medium, partially purified and characterized. The enzyme was inducible by both - and -tyrosine, although -tyrosine was the better inducer. The enzyme required -tyrosine and a-ketoglutarate as amino donor and amino acceptor, respectively. Its pH optimum in 50 m-potassium phosphate buffer was 7·6, the apparent Michaelis constants were 0·5 m for -tyrosine and 0·25 m for a-ketoglutarate; it had a molecular weight of 110000.

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/content/journal/micro/10.1099/00221287-128-11-2735
1982-11-01
2021-10-23
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