Purification and some properties of camel carboxypeptidase B |
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Authors: | Al-Ajlan Abdulrahman Bailey Graham S. |
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Affiliation: | (1) Department of Biological Sciences, Central Campus, University of Essex, Wivenhoe Park, Colchester, Essex, CO4 3SQ, UK |
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Abstract: | A carboxypeptidase B-like enzyme was purified 116-fold with a recovery of activity of 29% from a crude extract of camel pancreas by a four-step procedure consisting of two anion exchange chromatographies in succession, gel filtration and hydrophobic interaction chromatography. The enzyme was homogeneous on SDS and non-denaturing gel electrophoresis and on gel isoelectric focusing. Its molecular mass was found to be 31.5 kDa and its isoelectric point was estimated as 6.1. It was active towards a number of substrates that are cleaved by carboxypeptidases B from other species and was also susceptible to inhibition by inhibitors of such enzymes. The camel enzyme showed a pH optimum of 8.0 and it was seen to be a relatively potent kinase in vitro. The enzyme purified in this study was very similar to carboxypeptidases B isolated from other species in size, charge, substrate specificity and susceptibility to inhibition and thus it can be identified as camel carboxypeptidase B. |
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Keywords: | camel carboxypeptidase B purification characterization substrate specificity |
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