Purification and Characterization of an Iminopeptidase from the Primary Leaf of Wheat (Triticum aestivum L.) | Zendy

Stephen P. Waters | Zendy; Michael J. Dalling | Zendy

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Purification and Characterization of an Iminopeptidase from the Primary Leaf of Wheat (Triticum aestivum L.)

Author(s) -

Stephen P. Waters,

Michael J. Dalling

Publication year - 1983

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.73.4.1048

Subject(s) - proline , dipeptide , size exclusion chromatography , chemistry , hydroxyproline , hydrolysis , ion chromatography , substrate (aquarium) , primary (astronomy) , amino acid , chromatography , molecular mass , enzyme , biochemistry , biology , ecology , physics , astronomy

Iminopeptidase (EC 3.4.11.5) was substantially purified from the primary leaves of 7-day-old wheat seedlings (Triticum aestivum L.). The purification procedure consisted of five steps: acid precipitation, molecular exclusion chromatography on Sephacryl S-200, Ultrogel AcA 44, Sepharose 2B and ion-exchange chromatography on DEAE-cellulose. Iminopeptidase isolated in this manner was only active against the beta-naphthylamides of proline and hydroxyproline. For each substrate, the pH optimum was 7.4 and activity was sensitive to sulfhydryl group inhibitors. The iminopeptidase hydrolyzed the dipeptides Pro-Leu, Pro-Gly, Hyp-Gly, and Pro-Tyr. Iminopeptidase activity against the dipeptide Pro-Gly was higher than against Hyp-Gly. The molecular weight was estimated to be about 400,000. Evidence was obtained for the existence of endogenous inhibitors of iminopeptidase activity.

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