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ヒトデ消化系中のコンキオリン分解酵素について


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Title: ヒトデ消化系中のコンキオリン分解酵素について
Other Titles: A Study of the Chonchiolin-Decomposing Enzyme Present in the Digestive Organs of the Starfish
Authors: 石田, 忠 / 保田, 正人
Authors (alternative): Ishihara, Tadashi / Yasuda, Masato
Issue Date: Oct-1965
Publisher: 長崎大学水産学部
Citation: 長崎大学水産学部研究報告, v.19, pp.85-90; 1965
Abstract: An organic matter, which is present in small quantities in shells and pearls together with calcium carbonate, was named conchiolin by FREMY, and later, through the studies made by many researchers, it proved to be a kind of protein. The amino acid compositions and the structures of conchiolins, which are obtained from various species of molluscs, have been known to be different from one another. Few studies had been made on conchiolin till recently, but the development of the studies on pearls and the investigation on the calcium metabolism of molluscs-shells have promoted the studies on conchiolin. Nevertheless, very few studies have been reported on the enzymatic decomposition of conchiolin. It is a very interesting phenomenon in nature that shellfish are eaten away by other aquatic animals, for example, starfish or some snails. The authors have detected a kind of enzyme decomposing conchiolin in the digestive organs of starfish (Asterina pectinifera) and purified it by the salting-out method with ammonium sulfate and by the use of DEAE-cellulose columns. The authors also investigated enzymatic properties of the purified enzyme, namely the optimum pH and temperature and the effects of metal ions. / イトマキヒトデ消化系中にアサリ貝殻コンキオリンを分解する酵素の存在することを見いだしたので,その酵素の精製を硫酸アンモニウムによる塩析,およびDEAEセルロースカラムによって実施し,反応最適のpH,温度および金属イオンによる活性への影響について検討し,さらにペプシン・トリプシンとの比較を行なった結果,特異な酵素であることを知った. 1.アサリ貝殻コンキオリンに対する分解の最適pHは7.0~7.5である. 2.同じく最適温度は30~35℃の間にある. 3.金属イオン中Co⁺²またはMn⁺²は本酵素に対し活性化作用を持ち,前者には保護作用も認めた. 4.本酵素はペプシン,トリプシンよりもコンキオリン分解作用は大きく,カゼイン分解作用は小さい.
URI: http://hdl.handle.net/10069/31544
ISSN: 05471427
Type: Departmental Bulletin Paper
Text Version: publisher
Appears in Collections:第19号

Citable URI : http://hdl.handle.net/10069/31544

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