@article{oai:kpu.repo.nii.ac.jp:00004891,
 author = {三好, 正満 and Miyoshi, Masamitsu and 伊吹, 文男 and Ibuki, Fumio and 金森, 正雄 and Kanamori, Masao},
 journal = {京都府立大學學術報告. 農學, The scientific reports of Kyoto Prefectural University. Agriculture},
 month = {Oct},
 note = {Succinic anhydrideによってκ-カゼインのアミノ基を4.8∿93.2%修飾したサンプルを用いて, α_S-カゼイン安定化力, 構成成分の被修飾性, 等電点変化, 会合度変化, Caとの反応性を調べた。α_S-カゼイン安定化力は, 8.8%修飾までは変化なく, 15.9∿19.6%修飾で次第に低下し, 32.3%修飾で完全に消失した。このように最も反応性に富んだアミノ基がα_S-カゼイン安定化力に無関係である事実は, κ-カゼインのアミノ基は直接α_S-カゼインとのミセル形成に関係していないことを意味するものと考えられる。還元κ-カゼインの電気泳動の結果, κ-カゼイン構成成分のうち尿素中でpH6付近に等電点を持つ成分がpH5付近の成分より, より早く修飾されることが判明した。したがって, より中性側に等電点を持つ成分がκ-カゼインの表面構造を形成しているものと推定された。サクシニル化に伴なって等電点が酸性側へ移行し, 尿素中における等電点がα_S-カゼインのそれと同じpH5付近になると, Caとの反応性が低下し, α_S-カゼインを安定化する能力が完全に失なわれた。, Amino groups of κ-casein were succinylated at pH8 to various degrees ranging from 4.8 to 93.2 percent. These modified κ-caseins were used for α_S-casein stabilizing test in the presence of 0.02M calcium chloride. The ability of κ-casein to stabilize α_S-casein did not change up to 8.8 percent succinylation, but decreased gradually as the modification reaction proceeded further until 32.3 percent succinylation, where the α_S-casein stabilizing ability of κ-casein completely disappeared. The initial succinylation of amino groups occurred on specific residues rather than in a random fashion among all the free residues. At pH8,the κ-casein components with isoelectric points at pH5.8 and 6.1 in 6M urea were, in the early stage of succinylation, modified more rapidly than the rest with isoelectric points on more acidic side. It indicates that the κ-casein components with their pIs around pH6 are located in the external hydrophilic region of κ-casein complex, and that they probably play important roles in the interaction with α_S-casein which brings about the stabilization of α_S-casein in the presence of calcium chloride. As previously reported, κ-casein lost its ability to stabilize α_S-casein when the isoelectric point moved to pH5.0-5.2,that of α_S-casein, in 6M urea as a result of succinylation.},
 pages = {155--162},
 title = {Studies on κ-Casein of Bovine Milk VI : Reduced components and the α_S-casein stabilizing ability of succinylated κ-casein (Agricultural Chemistry)},
 volume = {23},
 year = {1971},
 yomi = {ミヨシ, マサミツ and イブキ, フミオ and カナモリ, マサオ}
}