Choubey, Divaker and Gopinathan, KP (1986) Characterization of beta-lactamase from Mycobacterium smegmatis SN2. In: Current Microbiology, 13 (3). pp. 171-175.
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beta-Lactamase from Mycobacterium smegmatis SN2 was purified to homogeneity. The molecular weight of the enzyme was 30,000 and the isoelectric point was 4.1. The enzyme showed maximal activity at pH 6.5 and 56~ and resembled the plasmid-mediated TEM-type beta-lactamases commonly encountered in gram-negative bacteria in substrate profile. The enzyme shared antigenic structure with beta-1actamase from Mycobacterium butyricum ATCC 19979 and Escherichia coli HB101 (pBR322).
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Springer.|
|Department/Centre:||Division of Biological Sciences > Microbiology & Cell Biology|
|Date Deposited:||10 Aug 2009 08:37|
|Last Modified:||19 Sep 2010 05:40|
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