著者
MORITA Shimpei FUKASE Masami HOSHINO Kumiko FUKUDA Yoichi YAMAGUCHI Masami MORITA Yuhei
出版者
Japanese Society of Plant Physiologists
雑誌
Plant and cell physiology (ISSN:00320781)
巻号頁・発行日
vol.35, no.7, pp.1049-1056, 1994-10
参考文献数
38
被引用文献数
6

A proteolytic activity directed against the a subunit of β-conglycinin was detected in resting mature seeds of the soybean [Glycine max (L.) Merrill] cultivar Keburi. The relationship between pH and activity and the effect of protease inhibitors revealed that the enzyme was a neutral/alkaline serine protease. The proteolysis of the a subunit of β-conglycinin yielded a specific product with a molecular weight of about 47,000, as determined by SDS-PAGE, but the enzyme had no activity against the β subunit. The amino acid composition, the molecular weight and the amino-terminal amino acid sequence of the proteolytic product revealed that the action of the enzyme on the a subunit was specific, with cleavage occurring only at the R126-R127 peptide bond of the a subunit. These characteristics of the protease indicate that the enzyme is a novel protease that has not previously been recognized in soybean seeds.

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