title: Purification and some properties of camel carboxypeptidase B.
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 kininase 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.
authors.affiliation: Department of Biological Sciences, Central Campus, University of Essex, Colchester, UK.
authors.forename: A
authors.initials: A
authors.lastname: Al-Ajlan
authors.forename: G S
authors.initials: GS
authors.lastname: Bailey
mesh_terms: D000818:Animals; D002162:Camelus; D043424:Carboxypeptidase B; D002268:Carboxypeptidases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism*; D002852:Chromatography, Ion Exchange / Q000379:methods; D004492:Edetic Acid / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D010179:Pancreas / Q000201:enzymology; D013379:Substrate Specificity
chemical_list: D004791:Enzyme Inhibitors; D004492:Edetic Acid; D002268:Carboxypeptidases; D043424:Carboxypeptidase B