Further Characterization of a Sarcoplasmic Serine Proteinase from the Skeletal Muscle of White Croaker (Argyrosomus argentatus)

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Min-Jie Cao^1*, Kenji Hara², Ling Weng¹, Nong Zhang³, and Wen-Jin Su¹

¹College of Biological Engineering, Jimei University, Jimei, Xiamen, 361021, China; fax: +86-592-6180470; E-mail: mjcao@jmu.edu.cn

²Faculty of Fisheries, Nagasaki University, Nagasaki, 852-8521, Japan

³Fisheries Research Institute of Fujian Province, Xiamen, 361012, China

^* To whom correspondence should be addressed.

Received September 21, 2004; Revision received October 21, 2004

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A trypsin-type serine proteinase (WSP) was purified previously from the sarcoplasmic fraction of skeletal muscle of white croaker (Argyrosomus argentatus) by Yanagihara et al. ((1991) Nippon Suisan Gakaishi, 57, 133-142). However, further research on WSP was not carried out. In the present study, we determined the N-terminal amino acid sequence of this enzyme (27 amino acid residues), which revealed relatively high identity in the conserved region to other trypsin-type serine proteinases. Degradation action of WSP on neuropeptides is also reported in this manuscript. The results show that WSP only cleaves at the carboxyl side of Arg or Lys residue of the peptides, especially between dibasic amino acid residues such as Arg-Arg and Arg-Lys.

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KEY WORDS: amino acid sequence, white croaker, serine proteinase, dibasic, identity, peptide

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