Thermal Stability of Two Heterotrimeric Molecular Forms of the Quantitatively Major Collagen from the Kuruma Prawn Muscle
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- Mizuta Shohshi
- Department of Marine Bioscience, Faculty of Biotechnology, Fukui Prefectural University
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- Yoshinaka Reiji
- Department of Marine Bioscience, Faculty of Biotechnology, Fukui Prefectural University
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- Sato Mamoru
- Faculty of Fisheries, Kagoshima University
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- Sakaguchi Morihiko
- Department of Fisheries, Faculty of Agriculture, Kyoto University
書誌事項
- タイトル別名
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- Thermal Stability of Two Heterotrimeric
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Thermal stability of the pepsin-solubilized Type AR-I collagen was estimated by monitoring the protease-induced degradation of helical domains by SDS-PAGE. The pepsin-solubilized Type AR-Ia collagen, designated as [α1(AR-I)]3, denatured at 34.7°C. On the other hand, the α1(AR-I) and α2(AR-I) components in the mixture of the pepsin-solubilized Type AR-Ib and AR-Ic collagens, [α1(AR-I)]2 α2(AR-I) and α1(AR-I)[α2(AR-I)]2, respectively, showed transition midpoints of 33.5 and 33.8°C, respectively. From these results, the pepsin-solubilized Type AR-Ib and AR-Ic collagens were less stable to heat than the pepsin-solubilized Type AR-Ia collagen. In addition, the α2(AR-I) component in the intact Type AR-Ib and AR-Ic collagens in the residual fraction after alkali (0.1 N NaOH) extraction from muscular tissue showed an approximate transition midpoint of 37.9°C. These combined resultssuggest that the thermal stability of intact Type AR-Ib and AR-Ic collagens are considerably reduced by pepsin digestion which causes the removal of their telopeptides and change of their molecular properties such as molecular arrangement or solubility.
収録刊行物
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- Fisheries science
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Fisheries science 62 (4), 577-581, 1996
公益社団法人 日本水産学会
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詳細情報 詳細情報について
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- CRID
- 1390282679406852224
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- NII論文ID
- 130003742028
- 10004866819
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- NII書誌ID
- AA10993718
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- NDL書誌ID
- 4014513
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- ISSN
- 09199268
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
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- 抄録ライセンスフラグ
- 使用不可