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Bioscience, Biotechnology, and Biochemistry | 1996

Oryzacystatins exhibit growth-inhibitory and lethal effects on different species of bean insect pests, Callosobruchus chinensis (Coleoptera) and Riptortus clavatus (Hemiptera).

Masaharu Kuroda; Masao Ishimoto; Kazunori Suzuki; Hiroto Kondo; Keiko Abe; Keisuke Kitamura; Soichi Arai

Oryzacystatins I and II, cysteine proteinase inhibitors in rice seeds, caused growth retardation of different species of bean insect pests, Callosobruchus chinensis (Coleoptera) and Riptortus clavatus (Hemiptera), when added to their diets at concentrations of 0.3-0.5% (w/w). At concentrations of up to 1%, almost all insects died. Our results suggest the usefulness of cystatin for insect pest control and also the critical role of cysteine proteinase in the digestive events of insects.


FEBS Letters | 1992

Inhibitory effect of oryzacystatins and a truncation mutant on the replication of poliovirus in infected Vero cells

Hiroto Kondo; Sumiko Ijiri; Keiko Abe; Hiroshi Maeda; Soichi Arai

Poliovirus, a picornavirus family member, requires the processing of its poly‐protein by its own cysteine proteinase for replication. Oryzacystatin‐I and oryzacystatin‐II, proteinaceous cysteine proteinase inhibitors (cystatins) of rice seed origin, were found to inhibit the replication of poliovirus effectively in infected Vero cells in vitro. Truncated oryzacystatin‐I, which lacks the NH2‐terminal 25 amino acid residues of the intact protein, is an even more effective inhibitor, eliciting its effect at concentrations of less than 0.23 nmol/ml. The low molecular weight cysteine proteinase inhibitors, E‐64, E‐64C and loxistatin, showed no anti‐viral effect at any concentration investigated.


Journal of Biological Chemistry | 1987

Molecular cloning of a cysteine proteinase inhibitor of rice (oryzacystatin). Homology with animal cystatins and transient expression in the ripening process of rice seeds.

Keiko Abe; Yasufumi Emori; Hiroto Kondo; Koichi Suzuki; Soichi Arai


Journal of Biological Chemistry | 1990

Two distinct cystatin species in rice seeds with different specificities against cysteine proteinases. Molecular cloning, expression, and biochemical studies on oryzacystatin-II.

Hiroto Kondo; Keiko Abe; I Nishimura; Hiroshi Watanabe; Yasufumi Emori; Soichi Arai


Agricultural and biological chemistry | 1987

Purification and Characterization of a Rice Cysteine Proteinase Inhibitor

Keiko Abe; Hiroto Kondo; Soichi Arai


Journal of Biochemistry | 1991

Papain-inhibitory activity of oryzacystatin, a rice seed cysteine proteinase inhibitor, depends on the central Gln-Val-Val-Ala-Gly region conserved among cystatin superfamily members

Soichi Arai; Hirohito Watanabe; Hiroto Kondo; Yasufumi Emori; Keiko Abe


Journal of Biological Chemistry | 1988

The NH2-terminal 21 amino acid residues are not essential for the papain-inhibitory activity of oryzacystatin, a member of the cystatin superfamily. Expression of oryzacystatin cDNA and its truncated fragments in Escherichia coli.

Keiko Abe; Yasufumi Emori; Hiroto Kondo; Soichi Arai; Koichi Suzuki


Biomedica biochimica acta | 1991

Oryzacystatins as the first well-defined cystatins of plant origin and their target proteinases in rice seeds.

Keiko Abe; Hiroto Kondo; Hirohito Watanabe; Yasufumi Emori; Soichi Arai


Agricultural and biological chemistry | 1987

Purification and Properties of a Cysteine Proteinase from Germinating Rice Seeds

Keiko Abe; Hiroto Kondo; Soichi Arai


Journal of Biochemistry | 1998

SUBSTRATE SPECIFICITIES AND KINETIC PROPERTIES OF PROTEINASE A FROM THE YEAST SACCHAROMYCES CEREVISIAE AND THE DEVELOPMENT OF A NOVEL SUBSTRATE

Hiroto Kondo; Yuji Shibano; Teruo Amachi; Nora Cronin; Kohei Oda; Ben M. Dunn

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