@article{oai:kpu.repo.nii.ac.jp:00005525,
 author = {大槻, 耕三 and Otsuki, Kozo and 三宅, 智恵子 and Miyake, Chieko and 佐藤, 健司 and Sato, Kenji and 河端, 信 and Kawabata, Makoto},
 journal = {京都府立大学学術報告. 理学・生活科学, The scientific reports of the Kyoto Prefectural University. Natural science and living science},
 month = {Nov},
 note = {Kiwifruit protease (EC 3. 4. 22. 14) was purified with conventional DEAE-cellulose and Octyl-Sepharose, a packing material of hydrophobic chromatography. With these methods, a rapid purification or concentration of the enzyme was obtained. The partially purified protease was further purified and successfully separated on the column of Bakerbond WP-PEI with a lineargradient elution of 0-0.75M NaCl into two enzymes, A_1 and A_2,which were named by Mcdowall (Biochim. Biophys. Acta, 293,226 (1973)). Kiwifruit proteases A_1 and A_2 were purified to 90% and 93% homogeneity of mol. wt. as checked by TSK G2000SW XL gel-chromatography.},
 pages = {37--41},
 title = {キーウィフルーツ・プロテアーゼの分離・精製 : 新しいイオン交換充填剤 Bakerbond WP-PEI による分離(B. 生活科学)},
 volume = {44},
 year = {1993},
 yomi = {オオツキ, コウゾウ and ミヤケ, チエコ and サトウ, ケンジ and カワバタ, マコト}
}