The Carboxyl-Terminal Half-Molecule of Ovotransferrin Prepared by Selective Digestion of the Amino-Terminal Lobe with Thermolysin
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概要
- 論文の詳細を見る
Diferric ovotransferrin was hydrolyzed by thermolysin, a thermostable protease, at elevated temperatures. At 65℃, the amino(N)-terminal lobe was completely digested into small peptides, while the carboxyl(C)-terminal lobe was significantly resistant to the protease. This permitted the isolation of an iron-bound C-terminal half-molecule consisting of a glycosylated single polypeptide in an excellent yield (about 90%). The fragment comprises the residoes from 336 to the C-terminus of ovotransferrin. The results for the visible absorpdon spectrum of the copper-bound fragment, the stability of the iron-bound fragment in high concentration of urea, and the CD spectra of the fragment in the far and near UV regions indicated that it retains the metal binding activity and conformation of the C-terminal lobe of intact ovotransferrin.
- 社団法人日本農芸化学会の論文
- 1992-01-23
著者
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Enami Isao
Department Of Biology Faculty Of Science Science University Of Tokyo
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Enami Isao
Department Of Biology Science University Of Tokyo Kagurazaka
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Kondo Kiyoshi
Research Institute For Biosciences Science University Of Tokyo
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Satake Kazuo
Department Of Chemistry Faculty Of Science Science University Of Tokyo Kagurazaka
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Satake Kazuo
Department Of Biochemistry Faculty Of Science Tokyo Metropolitan University
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Tsugita A
Research Institute For Biosciences Science University Of Tokyo
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Tsugita Akira
Research Institute For Biosciences Science University Of Tokyo
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NAKAZATO Katsuyoshi
Department of Biology, Science University of Tokyo, Kagurazaka
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Nakazato Katsuyoshi
Department Of Biology Science University Of Tokyo Kagurazaka
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