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Metabolism and Enzymology

Characterization of the Major Protease Involved in the Soybean -Conglycinin Storage Protein Mobilization ¹

Department of Biological Sciences, State University of New York at Binghamton, P.O. Box 6000, Binghamton, New York 13902-6000

Protease C1, the protease responsible for the initial degradation of the ' and subunits of the soybean -conglycinin storage protein (Glycine max [L.] Merrill), has been purified. The enzyme was found by sodium dodecyl sulfate-polyacrylamide gel electrophoresis to have a molecular weight of 70,000 and a pH optimum of 3.5 to 4.5. Susceptibility to protease inhibitors indicates that protease C1 is a serine protease. Study of the proteolytic intermediates generated suggests that the cleavage of the ' and subunits of -conglycinin by protease C1 results in intermediates that are 1 or 2 kilodaltons smaller than the native ' and subunits. Following that, a succession of intermediates exhibiting molecular masses of 70.0 and 58.0 kilodaltons, then 63.0, 61.0, 55.0, and 53.5 kilodaltons, are observed. A 50.0- and a 48.0- kilodalton intermediate are the final products of protease C1 action. Comparison of these intermediates with the prominent anti--conglycinin cross-reacting bands that increase during the first few days of germination and early growth show that protease C1 plays an important physiological role, but not an exclusive one, in the living plant.

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