Accession Number:

AD0620596

Title:

BENZYLAMINE OXIDASE AND HISTAMINASE: PURIFICATION AND CRYSTALLIZATION OF AN ENZYME FROM PIG PLASMA,

Descriptive Note:

Corporate Author:

OXFORD UNIV (ENGLAND) DEPT OF PHARMACOLOGY

Personal Author(s):

Report Date:

1964-04-09

Pagination or Media Count:

19.0

Abstract:

The enzyme benzylamine oxidase of pig plasma was purified and some of the properties of the pure preparation were studied. The purification procedure included several precipitations with ammonium sulphate and separations of proteins by column chromatography, first on DEAEcellulose, followed by DEAE-Sephadex and lastly on a hydroxy-apatite column. Crystals were prepared from solutions of the purified enzyme by adding ammonium sulphate. The crystalline preparation was homogeneous when studied by starch-gel electrophoresis and by ultracentrifugation. The molecular weight, as determined on the analytical ultracentrifuge, was 195000. The copper content of the enzyme, as determined by radioactivation analysis, was about four atoms of Cu per molecule of enzyme. Concentrated solutions of the enzyme had a pink colour the colour disappeared when substrate benzylamine was added under anaerobic conditions. The amines which were tested and found to be oxidized by the pure enzyme were benzylamine, histamine, mescaline and 4-picolylamine. The affinity of the enzyme for benzylamine was more than one hundred times that for histamine. Author

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Distribution Statement:

APPROVED FOR PUBLIC RELEASE