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Biochim Biophys Acta ; 1670(1): 84-9, 2004 Jan 05.
Article in English | MEDLINE | ID: mdl-14729145

ABSTRACT

A cDNA clone encoding a novel papain-like cysteine protease was isolated from wheat germ (Triticum aestivum). This cDNA encoded a 371-residue protein, designated WCP2, composed of signal peptide followed by a propeptide and a mature protease containing active site residues that are highly conserved among the papain family. The mature WCP2 protein (26 kDa) was detected in the quiescent embryo and its level of expression in the germinating embryo was greatly increased.


Subject(s)
Cysteine Endopeptidases/genetics , Gene Expression Regulation, Enzymologic , Triticum/enzymology , Amino Acid Sequence , Base Sequence , Cloning, Molecular , Cysteine Endopeptidases/biosynthesis , DNA, Complementary/biosynthesis , Germination , Molecular Sequence Data , Sequence Alignment
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