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Biochemistry, Biophysics, and Structural Biology Commons

Open Access. Powered by Scholars. Published by Universities.®

Biotechnology

University of Nebraska - Lincoln

1981

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Full-Text Articles in Biochemistry, Biophysics, and Structural Biology

Peptidohydrolases Of Soybean Root Nodules, Nasir S. A. Malik, N. E. Pfeiffer, D. R. Williams, Fred W. Wagner Jan 1981

Peptidohydrolases Of Soybean Root Nodules, Nasir S. A. Malik, N. E. Pfeiffer, D. R. Williams, Fred W. Wagner

Biochemistry -- Faculty Publications

Nodule extracts prepared from Glycine max var Woodworth possessed endopeptidase, aminoptidase, and carboxypeptidase actiities. Three distinct endopeptidase activities could be resolved by disc-gel electrophoresis at pH 8.8. According to their order of increasing electrophoretic mobility, the first of these enzymes hydrolyzed azocasein and n-benzoyl-LLeu-β-naphthylamide, while the second hydrolyzed n-benzoyl-L-Arg-/8- naphthylamine (Bz-L-Arg-/βNA), n-benzoyl-L-Arg-β-nitroanilide (Bz-L-Arg-βNA), and azocasein. The third endopeptidase hydrolyzed Bz-L-Arg-βNA, Bz-L-Arg-βNA, and hemoglobin. Fractions of these enzymes extracted from electrophoresis gels were shown to have pH optima from 7.5 to 9.8. AU of the endopeptidases were completely inhibited by diisopropylphosphorofluoridate, demonstrating that they were serine ...