Arch Biochem Biophys. 1986 Nov 1;250(2):322-8.

Purification and characterization of mandelonitrile lyase from Prunus lyonii.

Abstract

The enzyme mandelonitrile lyase (EC 4.1.2.10) which catalyzes the decomposition of the cyanohydrin of benzaldehyde has been isolated and purified to homogeneity from mature seeds of the California cherry (Prunus lyonii). The purification procedure involved chromatography on DEAE-cellulose and Con-A-Sepharose with a final recovery of 60% of enzyme activity. Purification of only 4.3-fold yielded a nearly homogeneous preparation. The absorption spectrum of this protein shows maxima at 278, 389, and 463 nm, indicative of its flavoprotein character. The native molecular weight for the lyase was found to be 50,000. The subunit molecular weight of 59,000 was estimated by gel electrophoresis in the presence of sodium dodecylsulfate. The isoelectric point was estimated to be 4.75. The enzyme has a narrow pH optimum around 5.5 and is highly stable at 4 degrees C.

PMID:: 3777939; [PubMed - indexed for MEDLINE]

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Research Support, U.S. Gov't, P.H.S.

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GM-05301-28/GM/NIGMS NIH HHS/United States

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Purification and characterization of mandelonitrile lyase from Prunus lyonii.

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Publication Types, MeSH Terms, Substances, Grant Support

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Cited by 3 PubMed Central articles

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