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. 1969 Apr;112(3):335–342. doi: 10.1042/bj1120335

Brain arylamidase. Purification and characterization of the soluble bovine enzyme

A S Brecher 1, J B Suszkiw 1
PMCID: PMC1187713  PMID: 5801305

Abstract

1. An enzyme acting on aminoacyl-β-naphthylamides has been isolated from the soluble fraction of bovine brain and purified 205-fold by means of ammonium sulphate fractionation, hydroxyapatite adsorption and DEAE-Sephadex column chromatography. 2. Arylamidase requires thiol groups for retention of its activity, is heat-labile and is susceptible to freezing. p-Chloromercuribenzoate and N-ethylmaleimide inactivate the enzyme rapidly. 3. Metal ions are not required for its activity, but stimulation by Mn2+ and Mg2+ and inactivation by Co2+ and Zn2+ are observed. 4. Optimum pH7·5 in phosphate buffer was exhibited for all substrates tested except l-leucyl-β-naphthylamide, for which optimum pH is 6·5. 5. Km values for a number of substrates have been obtained and substrate inhibition at high concentrations was demonstrated. 6. The molecular weight is approx. 70000 as determined by Sephadex-gel filtration.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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