Swaminathan, N. ; Radhakrishnan, A. N. (1969) Purification and properties of lactase from monkey kidney Biochimica et Biophysica Acta (BBA) - Enzymology, 191 (2). pp. 322-328. ISSN 0005-2744
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Official URL: http://linkinghub.elsevier.com/retrieve/pii/000527...
Related URL: http://dx.doi.org/10.1016/0005-2744(69)90251-4
Abstract
1. 1. Lactase activity is present in the particulate fraction obtained upon cnetrifugation of a homogenate of monkey kidney at 100 000 σ g for 60 min and could be solubilized by treatment with papain. The solubilized enzyme has been purified about 60-fold, and its properties have been studied. 2. 2. Lactose was the most active among a variety of substrates tested. Cellobiose and salicin showed, respectively, 20 and 16% of the activity using lactose. Other hetero-β-glucoside and -β-galactosides showed negligible activity. The purified lactase is strongly inhibited by glucono-(1 → 5)-lactone, while galactone-(1 → 4)-lactone inhibited to a much smaller extent.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to Elsevier Science. |
| ID Code: | 32426 |
| Deposited On: | 25 Apr 2011 12:44 |
| Last Modified: | 09 Jun 2011 11:45 |
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