|
type |
Journal Article |
authors |
Paszkowski, A.; Niedzielska, A. |
title |
Serine:glyoxylate aminotransferase from the seedlings of rye (Secale cereale L.) |
journal |
Acta Biochim Pol |
Activity |
2.6.1.45 |
ui |
91157551 |
year |
(1990) |
volume |
37 |
number |
2 |
pages |
277-82 |
| |
keywords |
Electrophoresis, Polyacrylamide Gel |
abstract |
Serine:glyoxylate aminotransferase (EC 2.6.1.45) from green parts of 7- day-old rye seedlings was purified 600-fold. Specific activity of the purified enzyme against L-serine and glyoxylate as substrates was 53.2 mumol/mg protein per minute at 30 degrees C. The enzyme activity with L- alanine or L-asparagine and glyoxylate, or with L-asparagine and hydroxypyruvate was 20% that with L-serine and glyoxylate as the amino group acceptor, whereas with L-alanine or glycine and hydroxypyruvate it was 10% of that value. The reaction rate with pyruvate and L- asparagine, glycine or L-serine was very low. The enzyme was stabilized by the presence of sucrose, pyridoxal phosphate and 2-mercaptoethanol. Molecular sieving of the native enzyme on Sephacryl S-300 gel gave Mr values of 91,200 and 85,000, whereas the molecular weight estimated by SDS-polyacrylamide gel electrophoresis was 43,000, indicating the dimeric structure of the enzyme. |
last changed |
2002/11/12 16:17 |
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