PURIFICATION OF ACYL HYDROLASE ENZYMES FROM THE LEAVES OF PHASEOLUS-MULTIFLORUS

被引：14

作者：

BURNS, DD ^{[1
]}

GALLIARD, T ^{[1
]}

HARWOOD, JL ^{[1
]}

机构：

[1] THE LORD RANK RES CTR,HIGH WYCOMBE HP12 3QR,BUCKINGHAMSHIRE,ENGLAND

来源：

PHYTOCHEMISTRY | 1979年 / 18卷 / 11期

关键词：

acyl hydrolase purification; Leguminosae; Phaseolus multiflorus; runner bean leaves; substrate specificities;

D O I：

10.1016/0031-9422(79)83054-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Acyl hydrolase activities have been purified from the leaves of Phaseolus multiflorus. The purification procedure involved heat treatment, DEAE-cellulose chromatography, Sephadex G-100 filtration and hexyl agarose chromatography. The elution pattern from hexyl agarose columns together with substrate competition experiments indicated the presence of two hydrolase enzymes. The first could hydrolyse oleoylglycerol and phosphatidylcholine while the second would deacylate glycosylglycerides and oleoylglycerol. Overall purification of both enzymes was ca 70-fold and the MW of the glycosylglyceride-hydrolysing enzyme was in the range 70-78000. © 1979.

引用

页码：1793 / 1797

页数：5

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