CORN KERNEL CYSTEINE PROTEINASE-INHIBITOR AS A NOVEL CYSTATIN SUPERFAMILY MEMBER OF PLANT-ORIGIN - MOLECULAR-CLONING AND EXPRESSION STUDIES

被引：155

作者：

ABE, M ^{[1
]}

ABE, K ^{[1
]}

KURODA, M ^{[1
]}

ARAI, S ^{[1
]}

机构：

[1] UNIV TOKYO, DEPT AGR CHEM, TOKYO 113, JAPAN

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1992年 / 209卷 / 03期

关键词：

D O I：

10.1111/j.1432-1033.1992.tb17365.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A full-length cDNA clone for a cysteine proteinase inhibitor (cystatin) was isolated from a lambdagt10 cDNA library of immature com kernels by screening with a mixture of cDNA inserts for oryzacystatins I and II. The cDNA clone spans 960 base pairs, encoding a 135-amino-acid protein containing a signal peptide fragment. The protein, named corn cystatin I, is considered to be a member of the cystatin superfamily, since it contains the commonly conserved Gln-Val-Val-Ala-Gly region that exists in most known cystatins as a probable binding site and is significantly similar to other cystatins in its overall amino acid sequence. Com cystatin I expressed in Escherichia coli showed a strong papain-inhibitory activity. Northern blot analysis showed that the amount of mRNA for com cystatin I reaches a maximum 2 weeks after flowering and then decreases gradually.

引用

页码：933 / 937

页数：5

共 23 条

[1]

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[2]

ABE K, 1987, J BIOL CHEM, V262, P16793

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