Purification of acyl hydrolase enzymes from the leaves of Phaseolus multiflorus |
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Authors: | D.Dougal Burns Terence Galliard John L. Harwood |
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Affiliation: | 1. Department of Biochemistry, University College, P.O. Box 78, Cardiff, CF1 1XL, U.K.;2. The Lord Rank Research Centre, High Wycombe, Bucks., HP12 3QR, U.K. |
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Abstract: | 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. |
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Keywords: | Leguminosae runner bean leaves acyl hydrolase purification substrate specificities. |
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