An affinity column for the purification of prenyltransferases |
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| Authors: | D L Bartlett C H King C D Poulter |
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| Affiliation: | 1. Department of Toxicology, School of Chemical and Life Sciences, Jamia Hamdard, New Delhi 110062, India;2. Division of Basic Medical Sciences, Indian Council of Medical Research, Government of India, V. Ramalingaswamy Bhawan, New Delhi 110029, India;3. Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Jamia Hamdard, New Delhi 110062, India;1. Max Planck Institute for Human Development, Max Planck Research Group Naturalistic Social Cognition, Lentzeallee 94, 14195 Berlin, Germany |
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| Abstract: | Farnesyl pyrophosphate synthetase (EC 2.5.1.1) from chicken liver, pig liver, and yeast has been purified to homogeneity in a single chromatographic step by affinity chromatography. The affinity ligand, geranylmethylphosphonophosphate, is linked to Affi-Gel 10 through the phosphonophosphate moiety. The affinity gel is stable chemically and the internal phosphonophosphate linkage is not hydrolyzed by nonspecific phosphatases. A single column has been used repeatedly for over a year with no degradation in its performance. A typical purification only requires 2 days and gives a 500- to 600-fold purification of enzyme from a crude ammonium sulfate precipitate. |
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