L-asparaginases from Mycobacterium tuberculosis strains H37Rv and H37Ra

Jayaram, H. N. ; Ramakrishnan, T. ; Vaidyanathan, C. S. (1968) L-asparaginases from Mycobacterium tuberculosis strains H37Rv and H37Ra Archives of Biochemistry and Biophysics, 126 (1). pp. 165-174. ISSN 0003-9861

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Official URL: http://dx.doi.org/10.1016/0003-9861(68)90570-5

Related URL: http://dx.doi.org/10.1016/0003-9861(68)90570-5

Abstract

M. tuberculosis H37Ra possesses two L-asparaginases while the H37Rv strain possesses only a single enzyme. These enzymes have been purified and their properties studied. The two L-asparaginases in H37Ra strain differ from each other in pH optima, heat inactivation, Michaelis constant and effects of inhibitors, while one of them resembles the single L-asparaginase present in the H37Rv strain. L-Cysteine inhibits both L-asparaginases in an allosteric manner probably because it is one of the end-products in L-asparagine metabolism. This is the first time that a qualitative difference has been reported in the enzyme pattern between the avirulent and virulent strains of M. tuberculosis.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
ID Code:49210
Deposited On:19 Jul 2011 11:45
Last Modified:01 Jul 2012 06:00

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