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