Limited proteolysis patterns of the B chain of insulin. |
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Authors: | D E Bowman |
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Affiliation: | Department of Biochemistry Indiana University School of Medicine Indianapolis, Indiana 46223 USA |
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Abstract: | The oxidized B chain of insulin was used as a simple model for further consideration of limited proteolysis with low substrate:enzyme ratios. With low B chain:trypsin ratios, the ordinarily slower cleavage rate of the -Lys29-Ala30 bond essentially equaled the cleavage saturation rate of the -Arg22-Gly23 bond. This led to the disappearance of octapeptide which ordinarily forms most rapidly. Heptapeptide and alanine, formed mainly by cleavage of the octapeptide, decreased somewhat at high enzyme relative levels. Trypsin added to B chain formed a single chromatographic peak. |
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Keywords: | NPGB p-nitrophenyl p′-guanidinobenzoate TPCK-trypsin trypsin treated with L-(tosylamido-2-phenyl) ethyl chloromethyl ketone S:E substrate: active enzyme molar ratio |
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