Choubey, Divaker ; Gopinathan, K. P. (1986) Characterization of β-lactamase from Mycobacterium smegmatis SN2 Current Microbiology, 13 (3). pp. 171-175. ISSN 0343-8651
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Official URL: http://www.springerlink.com/content/l18761574p5472...
Related URL: http://dx.doi.org/10.1007/BF01568514
Abstract
β -Lactamase fromMycohacterium smegamatis 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°C and resembled the plasmid-mediated TEM-type β -lactamases commonly encountered in gram-negative bacteria in substrate profile. The enzyme shared antigenic structure with β -lactamase from Mycobacterium butyricum ATCC 19979 and Escherichia coli HB101 (pBR322).
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to Springer Verlag. |
| ID Code: | 23667 |
| Deposited On: | 26 Nov 2010 08:49 |
| Last Modified: | 02 Jun 2011 06:17 |
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