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A serine proteinase from the sarcoplasmic fraction of red sea bream Pagrus major is possibly derived from blood


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Title: A serine proteinase from the sarcoplasmic fraction of red sea bream Pagrus major is possibly derived from blood
Authors: Yoshida, Asami / Bae, Inwoo / Sonoda, Hiroko / Cao, Min-Jie / Tachibana, Katsuyasu / Osatomi, Kiyoshi / Hara, Kenji
Issue Date: Oct-2009
Publisher: Springer Japan
Citation: Fisheries Science, 75(6), pp.1439-1444; 2009
Abstract: Collagen degradation is known to be involved in the post mortem tenderization of fish muscle. A serine proteinase that is assumed to be related to collagen degradation after fish death was purified from the sarcoplasmic fraction of red sea bream Pagrus major by ammonium sulfate fractionation and column chromatography on Sephacryl S-300, Q Sepharose and Phenyl Sepharose CL-4B. The enzyme hydrolyzed gelatin and was obtained as a protein band of approximately 38 kDa upon sodium dodecyl sulfate polyacrylamide gel electrophoresis under reducing conditions. The N-terminal amino acid sequence of the enzyme was determined for 32 residues. A protein that had the same N-terminal amino acid sequence as the enzyme for ten residues was purified from the serum of red sea bream and showed the same characteristics as the enzyme. Therefore, it is suggested that the serine proteinase migrates from the blood to muscle and degrades muscle proteins after the death of the fish.
Keywords: Gelatinolytic enzyme / Muscle / Red sea bream / Serine proteinase / Serum
URI: http://hdl.handle.net/10069/24409
ISSN: 09199268
DOI: 10.1007/s12562-009-0161-6
Rights: © The Japanese Society of Fisheries Science 2009 / The original publication is available at www.springerlink.com
Type: Journal Article
Text Version: author
Appears in Collections:Articles in academic journal

Citable URI : http://hdl.handle.net/10069/24409

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