|
|
||||||||
|
Plant Physiology 58:516-520 (1976) © 1976 American Society of Plant Biologists Purification and Properties of Two Proteolytic Enzymes with Carboxypeptidase Activity in Germinated Wheat 1a 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.
1 Paper 359 of the Canadian Grain Commission, Grain Research Laboratory, Winnipeg, Manitoba, Canada R3C 3G9.
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| ASPB Publications | PLANT PHYSIOLOGY | THE PLANT CELL | |
|---|---|---|---|