A 20-kDa Protein with the GTP-Binding and Trypsin Inhibitory Activities fromGlycine max | Zendy

Toshifumi Hirata | Zendy; Shunsuke Izumi | Zendy; Sei-ichiro Tsuji | Zendy

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A 20-kDa Protein with the GTP-Binding and Trypsin Inhibitory Activities fromGlycine max

Author(s) -

Toshifumi Hirata,

Shunsuke Izumi,

Sei-ichiro Tsuji

Publication year - 1999

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.63.1816

Subject(s) - glycine , trypsin , trypsin inhibitor , kunitz sti protease inhibitor , gtp' , biochemistry , amino acid , chemistry , peptide sequence , microbiology and biotechnology , enzyme , biology , gene

A 20-kDa protein (p20) with a GTP binding activity was purified from the cultured cells of Glycine max (soybean). The amino acid sequence of p20 showed 65% identity in a 23 amino acid overlap against the Kunitz-type trypsin inhibitor of soybean reported. Furthermore, it was found that a Kunitz-type soybean trypsin inhibitor of commercial origin also binds GTP.

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