Studies on fish muscle protease. VIII. On the existence of protease active in neutral pH range.
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- MAKINODAN Yasuo
- Dept. Fish., Fac. Agr., Kyoto Univ.
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- IKEDA Shizunori
- Dept. Fish., Fac. Agr., Kyoto Univ.
Bibliographic Information
- Other Title
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- 魚筋肉プロテアーゼの研究-VIII
- 魚筋肉プロテアーゼの研究-8-中性付近において活性を示すたん白質分解酵素の存在について〔英文〕
- ギョ キンニク プロテアーゼ ノ ケンキュウ 8 チュウセイ フキン ニ オイ
- On the Existence of Protease Active in Neutral pH Range
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Abstract
Neutral protease was seeked in carp and red sea bream muscles. Activity was determined by measuring Folin, Cu-Folin, and Ninhydrin values of the trichloroacetic acid filtrate of the reaction mixture. Optimum pH for casein hydrolysis at near neutral pH was recognizable at around 5.4 by each determination, but this activity was considered to be due to the usual cathepsin D. The hydrolysis of hemoglobin at neutral pH range was observed only by the Ninhydrin method and its optimum pH was near 7.0. This activity is considered to be a new protease in fish muscle which has not yet been reported.
Journal
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- NIPPON SUISAN GAKKAISHI
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NIPPON SUISAN GAKKAISHI 42 (6), 665-670, 1976
The Japanese Society of Fisheries Science
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Keywords
Details 詳細情報について
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- CRID
- 1390282681391056256
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- NII Article ID
- 130000920160
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- NII Book ID
- AN00193422
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- COI
- 1:CAS:528:DyaE28XkslCjtrc%3D
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- ISSN
- 1349998X
- 00215392
- http://id.crossref.org/issn/00215392
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- NDL BIB ID
- 1717001
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed