This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Preston, K. R. Articles by Kruger, J. E. Search for Related Content PubMed PubMed Citation Articles by Preston, K. R. Articles by Kruger, J. E. Agricola Articles by Preston, K. R. Articles by Kruger, J. E.

Articles

Purification and Properties of Two Proteolytic Enzymes with Carboxypeptidase Activity in Germinated Wheat ¹

^a Canadian Grain Commission, Grain Research Laboratory, Winnipeg, Manitoba, Canada R3C 3G9

Two proteolytic enzymes with carboxypeptidase activity have been isolated from a germinated wheat extract and partially characterized. Both enzymes rapidly released amino acids from hemoglobin and gluten and hydrolyzed carbobenzoxy-phenylalanylalanine. The enzymes were inhibited by diisopropylphosphofluoridate, but unaffected by salts, ethylenediaminetetraacetate, and sulfhydryl reagents at lower concentrations, and had molecular weights of approximately 55,000 and 61,000. Analysis of the hydrolysis products of hemoglobin and gluten indicated that both enzymes had broad specificities, including the ability to release proline.

This article has been cited by other articles:

				A. Drzymala and W. Bielawski Isolation and characterization of carboxypeptidase III from germinating triticale grains Acta Biochim Biophys Sin, January 1, 2009; 41(1): 69 - 78. [Abstract] [Full Text] [PDF]