Modori-inducing Proteinase Active at 50.DEG.C. in Threadfin Bream Muscle.
-
- Kinoshita Masato
- Department of Fisheries, Faculty of Agriculture, Kyoto University
-
- Toyohara Haruhiko
- Department of Fisheries, Faculty of Agriculture, Kyoto University
-
- Shimizu Yutaka
- Kobe-Gakuin Women's Junior College
-
- Sakaguchi Morihiko
- Department of Fisheries, Faculty of Agriculture, Kyoto University
Bibliographic Information
- Other Title
-
- 50°Cに至適温度域を持つイトヨリダイ戻り誘発プロテアーゼの存在
- 50℃に至適温度域を持つイトヨリダイ戻り誘発プロテアーゼの存在〔英文〕
- 50ドC ニ シテキ オンドイキ オ モツ イトヨリダイ モドリ ユウハツ プ
Search this article
Abstract
A novel modori-inducing proteinase optimally active at 50°C was purified to apparent homo-geneity from sarcoplasmic fraction of threadfin bream muscle using a combination of chromato-graphies on DEAE-cellulose, hydroxylapatite, Ultrogel AcA34, and TSK-gel G3000SWXL. This proteinase was distinguished from sarcoplasmic 60°C modori-inducing proteinase (Sp-60-MIP) purified from the same species in following points; (1) this novel proteinase degraded myosin heavy chain optimally at 50°C but did not do it at 60°C and (2) the molecular weight of this proteinase (500, 000) was higher than that of Sp-60-MIP (77, 000). However, this novel proteinase was found to share common properties with Sp-60-MIP in the respect of substrate specificity (trypsin-like) and inhibitor spectra (serine proteinase-like). This line of evidence suggests that trypsin-like serine proteinases play important roles in developing modori-phenomenon but major candidates for the phenomenon occurring at 50 and 60°C are clearly distinct.
Journal
-
- NIPPON SUISAN GAKKAISHI
-
NIPPON SUISAN GAKKAISHI 58 (4), 715-720, 1992
The Japanese Society of Fisheries Science
- Tweet
Keywords
Details 詳細情報について
-
- CRID
- 1390282681389794944
-
- NII Article ID
- 130001545601
-
- NII Book ID
- AN00193422
-
- COI
- 1:CAS:528:DyaK38Xkt1Cqt7c%3D
-
- ISSN
- 1349998X
- 00215392
- http://id.crossref.org/issn/00215392
-
- NDL BIB ID
- 3772650
-
- Text Lang
- en
-
- Data Source
-
- JaLC
- NDL
- Crossref
- CiNii Articles
-
- Abstract License Flag
- Disallowed