Cleavage specificity of cucumisin, a plant serine protease.

Cleavage specificity of cucumisin, a plant serine protease. Research Abstract Details 

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Cleavage specificity of cucumisin, a plant serine protease. Abstract Text:

T Uchikoba,H Yonezawa,M Kaneda,

Cucumisin was isolated from prince melon sarcocarp by means of a simple purification procedure. Serine protease inhibitors such as soybean trypsin inhibitor, ovomucoid, and aprotinin had no effect on the enzyme activity. alpha 2-Macroglobulin showed 38% inhibition of the original caseinolytic activity of cucumisin. The favorable synthetic substrates for cucumisin were Glt-Ala-Ala-Pro-Leu-pNA and Suc-Ala-Ala-Pro-Phe-pNA. The constant (kcat/Km) for Suc-Ala-Pro-Ala-pNA was found to be 30 times greater than that for Suc-Ala-Ala-Ala-pNA. The substrate specificity of cucumisin for oligopeptides and proteins was shown to be broad.

Cleavage specificity of cucumisin, a plant serine protease. Publishing Authors By Initials

T Uchikoba,H Yonezawa,M Kaneda,

For similar environment and public health: environment: environment, controlled: temperature research abstracts see: environment and public health: environment: environment, controlled: temperature research

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Cleavage specificity of cucumisin, a plant serine protease. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 117

Page Numbers: 1126-30

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: May

YEAR: 1995

Cleavage specificity of cucumisin, a plant serine protease. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Cleavage specificity of cucumisin, a plant serine protease. Keywords Mesh Terms:

KEYWORDS: Temperature

MESH TERMS: metabolism

Chemical & Substance for Abstract: Cleavage specificity of cucumisin, a plant serine protease. Information

Substance Name: cucumisin

Registry Number: EC 3.4.21.25

Grant and Affiliation Information for Cleavage specificity of cucumisin, a plant serine protease.

AFFILIATION: Department of Chemistry, Faculty of Science, Kagoshima University.

Country: JAPAN

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MEDLINETA: J Biochem

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