Studies on Carotenoprotein in Aquatic Animals : II Reddening of Carotenoprotein obtained from Crayfish (Cambarus clarkii)

広島大学水畜産学部紀要 Volume 11 Issue 2 Page 129-139 published_at 1972-12-20
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Title ( eng )
Studies on Carotenoprotein in Aquatic Animals : II Reddening of Carotenoprotein obtained from Crayfish (Cambarus clarkii)
Title ( jpn )
水産動物のカロチノプロテインに関する研究 : II アメリカザリガニのカロチノプロテインの赤変について
Creator
Nakagawa Heisuke
Kayama Mitsu
Asakawa Suezo
Source Title
広島大学水畜産学部紀要
Journal of the Faculty of Fisheries and Animal Husbandry, Hiroshima University
Volume 11
Issue 2
Start Page 129
End Page 139
Abstract
1. 天然の甲殻に存在する赤いカロチノプロテイン(R)は青又は紫カロチノプロテイン(B,P)の自動酸化により生じたものと考える.
2. RはB又はPを100℃に加熱して生じた赤いカロチノプロテイン(Rh)とは二・三性質を異にする.
3. B及びPの自動酸化,加熱により生ずるR,RhはB,Pよりカロチノイド含量が少なく,分子量は大きい.
4. B及びPを100℃加熱して生じたRhを長期間保存すると部分的ではあるが元のB,Pに回復することを認めた.
5. 0.005MのFe++,Fe+++,Sn++,Hg++,Cu++の存在によりカロチノプロテインは不可逆的に変性する.
1. The red carotenoprotein present in the native exoskeleton of the crayfish (Cambarus clarkii) seemed to be a derivative resulted from the oxidation of blue or purple carotenoproteins.

2. The red carotenoprotein extracted from the exoskeleton was different in physical properties from the reddened one resulted by boiling.

3. The red carotenoproteins resulted from boiling and autoxidation had a lesser carotenoid content and showed a higher molecular weight than the bluish carotenoproteins.

4. It was found that the carotenoprotein reddened by heating at 100°C was partially reconverted to the original bluish carotenoproteins.

5. The presence of 0.005 M Fe++, Fe+++, Sn++, Hg++, and Cu++ caused irreversible denaturation of the carotenoproteins.
NDC
Biology [ 460 ]
Language
eng
Resource Type departmental bulletin paper
Publisher
広島大学水畜産学部
Date of Issued 1972-12-20
Publish Type Version of Record
Access Rights open access
Source Identifier
[ISSN] 0440-8756
[NCID] AN00213563
[NAID] 40018463817