|
type |
Journal Article |
authors |
Sukanya, N. K.; Vaidyanathan, C. S. |
title |
Tryptophan-phenylpyruvate aminotransferase of Agrobacterium tumefaciens: purification and general properties of the enzyme |
journal |
J Ind Inst Sci |
Activity |
2.6.1.28 |
ui |
frhSxiFnd |
year |
(1979) |
volume |
61 |
number |
12 |
pages |
51-62 |
| |
keywords |
Agrobacterium/*enzymology |
abstract |
Tryptophan-phenylalanine aminotransferase (I) of A. tumefaciens was purified 67.5-fold with a yield of 90% from crude exts. and characterized. I had a pH optimum of 9.6 and showed significant activity at pH 10.6. The optimum temp. was 50°, with complete inactivation at 70°. This thermostability was increased in the presence of substrates of pyridoxal 5'-phosphate (II), the order of protection against heat denaturation being II > phenylpyruvate > tryptophan. I activity increased with increasing protein concn. from 10 to 100 mg. |
last changed |
2007/11/14 14:44 |
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