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Purification and some properties of camel carboxypeptidase B

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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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Authors and Affiliations

  1. Department of Biological Sciences, Central Campus, University of Essex, Wivenhoe Park, Colchester, Essex, CO4 3SQ, UK

    Abdulrahman Al-Ajlan & Graham S. Bailey

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  1. Abdulrahman Al-Ajlan
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  2. Graham S. Bailey
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Al-Ajlan, A., Bailey, G.S. Purification and some properties of camel carboxypeptidase B. Mol Cell Biochem 201, 105–110 (1999). https://doi.org/10.1023/A:1007012518250

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  • DOI: https://doi.org/10.1023/A:1007012518250

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