l-Asparaginase activity of soils
โ Scribed by W. T. Frankenberger; M. A. Tabatabai
- Publisher
- Springer
- Year
- 1991
- Tongue
- English
- Weight
- 626 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0178-2762
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๐ SIMILAR VOLUMES
The antineoplastic enzyme L-asparaginase is commonly used for the induction of remission in acute lymphoblastic leukemia (ALL). There is no simple method available for measuring the activity of this highly toxic drug. We incubated L-asparaginase from Erwinia chrysanthemi with L-aspartic acid โค-(7-am
A membrane-bound L-asparaginase (EC 3.5.1.1) of Tetrahymena pyriformis was purified to homogeneity. The purified enzyme is a lipoprotein, since it is inactivated by phospholipase C and its activity is restored by the addition of naturally occurring lipids, such as phosphatidylcholine, triolein and o
An automated method has been developed for the assay of L-asparaginase activity in plasma and other biological fluids. By means of this method, C asparaginase activity has been determined in plasma, cerebrospinal fluid, and urine in patients receiving E. coli L-asparaginase (EC-2) therapy. T h e hei
Most of L-asparaginase activity of Tetrahymena pyriformis was found to be present in microsomal membranes from which it has been purified to homogeneity (Tsirka, S.A.E. and Kyriakidis, D.A. Mol. Cell. Biochem. 83: 147-155, 1988). The native enzyme has a relative molecular weight of approximately 200