PURIFICATION OF PROTEIN CARBOXYMETHYLASE FROM OX BRAIN |
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| Authors: | M Iqbal T Steenson |
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| Institution: | Laboratory of Molecular Biophysics, Department of Zoology, University of Oxford, South Parks Road, Oxford, U.K.;Department of Biochemistry, Chelsea College, University of London, Manresa Road, London, SW3 6LX, U.K. |
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| Abstract: | Abstract— The enzyme protein carboxymethylase from the soluble fraction of ox brain was purified to electrophoretic homogeneity. Brain protein carboxymethylase activity was also detected in a membrane-bound form which could only be solubilized by treatment with detergent. The solubilized membrane-bound form differed from the 'native' soluble form in that the former irreversibly lost activity on removal of the detergent. The two forms, however, have several similarities, having a molecular weight of 35,000, a K m of 2.7 × 10?6 M for S -adenosyl-L-methionine, and a pH optimum of 6.2 when ovalbumin was used as the methyl acceptor. |
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