Degradation of β-Conglycinin β-Homotrimer by Papain: Independent Occurrence of Limited and Extensive Proteolysis
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概要
- 論文の詳細を見る
Limited and extensive proteolysis occur when β-conglycinin β homo-trimer (β3-conglycinin) from soybeans is attacked by papain. Slow limited proteolysis is restricted to cleavage of β3-conglycinin polypeptides into subunit halves (N- and C-terminal domains) that are further slightly truncated. The kinetics of limited and extensive proteolyses analyzed separately indicates that the two processes occur independently from the very beginning of the reaction. In contrast, limited proteolysis of phaseolin from common beans has been found to be prerequisite for the onset of its extensive proteolysis. The dramatic distinction between the degradation patterns of β3-conglycinin and phaseolin, homologous storage 7S globulins, suggests the existence of intrinsic differences in their structures. This hypothesis is supported by comparative analysis of the accessibilities to the solvent of amino acid residues in phaseolin and β3-conglycinin structures, which indicated the relatively low packing density of the latter, resulting in enhanced susceptibility of it to extensive proteolysis.
- 公益社団法人 日本農芸化学会の論文
著者
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Maruyama Nobuyuki
Laboratory Of Food Biochemistry Faculty Of Fisheries Hokkaido University
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Shutov Andrei
Laboratory Of Plant Biochemistry State University Of Moldova
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Rudakov Sergei
Laboratory Of Plant Biochemistry State University Of Moldova
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Rudakova Angela
Laboratory Of Plant Biochemistry State University Of Moldova
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WILSON Karl
Department of Biological Sciences, State University of New York at Binghamton
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KAKHOVSKAYA Irina
Laboratory of Plant Biochemistry, Moldova State University
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SCHALLAU Anna
Institute of Plant Genetics and Crop Plant Research (IPK)
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- Degradation of β-Conglycinin β-Homotrimer by Papain: Independent Occurrence of Limited and Extensive Proteolysis