Isolation of the S-peptide formed on digestion of fructose 1,6-bisphosphatase with subtilisin and its non-covalent association with the enzyme protein. |
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Authors: | A Dzugaj D K Chu H A El-Dorry B L Horecker |
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Affiliation: | Roche Institute of Molecular Biology Nutley, N. J. 07110 USA;Institute of Biological Chemistry University of Genoa Genoa, Italy |
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Abstract: | Digestion of rabbit liver fructose 1,6-bisphosphatase with subtilisin results in a several-fold increase in catalytic activity measured at pH 9.2. This change is due to cleavage of a peptide bond located 60 amino acid residues from the NH2-terminus. The S-peptide and the residual subunit appear as separate peptides in sodium dodecyl sulfate polyacrylamide gel electrophoresis and the S-peptide can be isolated by gel filtration in 9% HCOOH. Under nondissociating conditions, however, the S-peptide remains associated with the protein, and the tetrameric structure and original molecular weight are preserved. Thus the nicking of the peptide chain by subtilisin causes a conformation change that alters the catalytic properties of the enzyme. |
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