|
type |
Journal Article |
authors |
Rege, A. A. |
title |
Purification and characterization of a tyrosine aminotransferase from Crithidia fasciculata |
journal |
Mol Biochem Parasitol |
Activity |
2.6.1.5 |
Family |
2.6.1.5.a |
ui |
88038983 |
year |
(1987) |
volume |
25 |
number |
1 |
pages |
1-9. |
| |
keywords |
Animal |
abstract |
Tyrosine aminotransferase (TAT, EC 2.6.1.5) from the kinetoplastid, Crithidia fasciculata, was purified over 2000 fold to electrophoretic homogeneity. The native form of the enzyme had a molecular weight of approximately 100,000, whereas under denaturing conditions it produced two polypeptides of approximately 50,000 and 48,000, respectively. Absence of a reaction with the periodic acid-Schiff stain suggested that the crithidial enzyme was not a glycoprotein. It was relatively stable and remained active over a wide range of pH and temperature. It exhibited a broad substrate specificity and was able to utilize L- tyrosine, L-tryptophan, and L-phenylalanine as amino donors. Antiserum produced against partially purified crithidial tyrosine aminotransferase failed to inhibit the enzymatic activity. The same antiserum cross-reacted with a soluble extract from Trypanosoma brucei gambiense, but not with that from normal mouse liver, confirming evolutionary conservatism between the two protozoa. |
last changed |
2019/05/13 09:56 |
|