Selective cleavage of peptide bonds by a serine protease from rat skeletal muscle.

Selective cleavage of peptide bonds by a serine protease from rat skeletal muscle. Research Abstract Details 

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Selective cleavage of peptide bonds by a serine protease from rat skeletal muscle. Abstract Text:

K Kobayashi,Y Sanada,N Katunuma,

The selective cleavage of peptide bonds by a serine protease from skeletal muscle (SK-protease) was examined using glucagon and neurotensin as substrates. Among the peptide bonds cleaved in these substrates, the most susceptible were Phe-Thr-Ser, Tyr-Leu, Trp-Leu, and Tyr-Ile. These results indicate that the SK-protease hydrolyzed the carboxyl side of aromatic amino acid residues under the experimental conditions. When the amino acid on the carboxyl side of aromatic amino acid residues was serine, threonine or glutamic acid, these peptide bonds, such as Phe-Thr, Tyr-Ser, and Tyr-Glu, were not susceptible to another serine protease from small intestine (SI-protease) under the same experimental conditions. The peptide bond between the arginines of Pro-Arg-Arg-Pro in neurotensin was hydrolyzed by the SI-protease, but not by the SK-protease. Thus the specificity of the SK-protease differs from that of the SI-protease. These results suggest that the specificity of the hydrolytic action of the SK-protease is more like that of bovine chymotrypsin A than like that of porcine chymotrypsin C and of the SI-protease.

Selective cleavage of peptide bonds by a serine protease from rat skeletal muscle. Publishing Authors By Initials

K Kobayashi,Y Sanada,N Katunuma,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research

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Selective cleavage of peptide bonds by a serine protease from rat skeletal muscle. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 84

Page Numbers: 477-81

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Aug

YEAR: 1978

Selective cleavage of peptide bonds by a serine protease from rat skeletal muscle. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Selective cleavage of peptide bonds by a serine protease from rat skeletal muscle. Keywords Mesh Terms:

KEYWORDS: Substrate Specificity

MESH TERMS: metabolism

Chemical & Substance for Abstract: Selective cleavage of peptide bonds by a serine protease from rat skeletal muscle. Information

Substance Name: Chymotrypsin

Registry Number: EC 3.4.21.1

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Country: JAPAN

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MEDLINETA: J Biochem

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