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Corn kernel cysteine proteinase inhibitor as a novel cystatin superfamily member of plant origin. Molecular cloning and expression studies.

Eur. J. Biochem.1992 Nov 01;209(3):933-7. doi:10.1111/j.1432-1033.1992.tb17365.x
M Abe 1 , K Abe , M Kuroda , S Arai
M Abe 1 , K Abe , M Kuroda , S Arai

[No authors listed]

Author information
  • 1 Laboratory for Food Science, Gakushuin Women's Junior College, Tokyo, Japan.

摘要


A full-length cDNA clone for a cysteine proteinase inhibitor (cystatin) was isolated from a lambda gt10 cDNA library of immature corn 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. Corn cystatin I expressed in Escherichia coli showed a strong papain-inhibitory activity. Northern blot analysis showed that the amount of mRNA for corn cystatin I reaches a maximum 2 weeks after flowering and then decreases gradually.