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Plant and Cell Physiology, 1984, Vol. 25, No. 5 731-737
© 1984

Article

Purification and Characterization of an Aminopeptidase, LPAase 2, from Euonymus Leaves

Kiyoshi Tazaki and Nariyuki Ishikura1

Department of Biology, Faculty of Science, Kumamoto University Kumamoto 860, Japan

1To whom correspondence should be addressed.

An aminopeptidase, LPAase 2, from the leaves of Euonymus alatus f. ciliato-dentatus was purified about 240-fold by a combination of DEAE-cellulose and Sephadex G-100 column chromatographies. The molecular weight of LPAase 2 was estimated to be about 62,000, and the optimum pH for the hydrolytic activity against leucinep-nitroanilide (LPA) was 7.6. LPAase 2 hydrolyzed LPA, leucine-rß-naphthylamide (leucine-NA), phenylalanine-NA and tyrosine-NA. It was inhibited strongly by p-chloromercuribenzoate (PCMB), iodoacetic acid and heavy metal ions, but was not affected by thiol compounds and metal-chelating reagents. Therefore, a sulfhydryl group could be involved in the active site of LPAase 2. None of the metal ions tested promoted LPAase 2 activity. The properties of LPAase 2 were compared with those of aminopeptidases reported for other plants.

(Received November 24, 1983; Accepted April 16, 1984)
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