AMINOPEPTIDASE FROM THE COTYLEDONS OF VICIA FABA L. VAR. MINOR SEEDS: PARTIAL PURIFICATION AND SOME PROPERTIES

Authors


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    Abbreviation: INRA, Institut National de la Recherche Agronomique; LAPase, leucine aminopeptidase; DTT, dithiothreitol; ME, mercaptoethanol; Leu-p-N, leucine-para-nitroanilide; SDS-PAGE, sodium dodecylsulphate polyacrylamide gel electrophoresis; MW, molecular weight; BSA, bovine serum albumin.

Summary

Leucine aminopeptidase from field beans was studied in the cotyledons of dry and germinating seeds. The partially purified enzyme had a molecular weight of about 60000 (determined by gel filtration). Activity was maximal at pH 7.5, with leucine-p-nitroanilide or leucine naphthylamide as substrates, and was stimulated by dithiothreitol and mercaptoethanol and inhibited by Cu and Zn ions. During germination, the highest enzyme activity in the cotyledons occurred after 2d.

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