Hiremath, S. T. ; Paranjpe, Shaila ; SivaRaman, C. (1976) Purification and properties of citrate lyase from Streptococcus faecalis Biochemical and Biophysical Research Communications, 72 (3). pp. 1122-1128. ISSN 0006-291X
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Official URL: http://www.sciencedirect.com/science/article/pii/S...
Related URL: http://dx.doi.org/10.1016/S0006-291X(76)80248-3
Abstract
Citrate lyase from Streptococcus facealis has been purified to homogeneity. The enzyme has a molecular weight of about 580 000 and contains 3 non-identical subunits of about 53 000, 37 000 and 14 000 daltons. The subunits are not linked by interpeptide disulfide bridges. The enzyme does not dissociate in buffers of low ionic strength. The enzyme shows only a weak reaction inactivation and the enzyme complex is not associated with acetylating enzyme activity for reactivation of the HS-citrate lyase in presence of acetate and ATP.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to Elsevier Science. |
| ID Code: | 53488 |
| Deposited On: | 10 Aug 2011 09:51 |
| Last Modified: | 10 Aug 2011 09:51 |
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