Choubey, D. ; Gopinathan, K. P. (1986) Characterization of beta-lactamase from Mycobacterium butyricum ATCC 19979 Biochemistry International, 12 (2). pp. 207-214. ISSN 0158-5231
Full text not available from this repository.
Abstract
Beta-lactamase has been purified to a homogeneous state from Mycobacterium butyricum ATCC 19979. The molecular weight (Mr = 29,000) and the isoelectric point (4,0) of the enzyme have been determined. The enzyme showed both penicillinase and cephalosporinase activity, but had relatively more of the former. With respect to substrate-profile the enzyme resembled the plasmid specified TEM-type beta-lactamases commonly encountered in Gram-negative bacteria. The enzyme was insensitive to p-chloromercuribenzoate, sodium chloride, or iodine inhibition.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to International Union of Biochemistry. |
| ID Code: | 88091 |
| Deposited On: | 27 Mar 2012 08:17 |
| Last Modified: | 27 Mar 2012 08:17 |
Repository Staff Only: item control page
