title: Further characterization of a sarcoplasmic serine proteinase from the skeletal muscle of white croaker (Argyrosomus argentatus).
abstract: 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.
authors.affiliation: College of Biological Engineering, Jimei University, Jimei, Xiamen, 361021, China. mjcao@jmu.edu.cn
authors.forename: Min-Jie
authors.initials: MJ
authors.lastname: Cao
authors.forename: Kenji
authors.initials: K
authors.lastname: Hara
authors.forename: Ling
authors.initials: L
authors.lastname: Weng
authors.forename: Nong
authors.initials: N
authors.lastname: Zhang
authors.forename: Wen-Jin
authors.initials: WJ
authors.lastname: Su
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D004151:Dipeptides / Q000737:chemistry; D004795:Enzyme Stability; D008969:Molecular Sequence Data; D018482:Muscle, Skeletal / Q000201:enzymology*; D010473:Perciformes; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*; D012697:Serine Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology*; D013379:Substrate Specificity; D013997:Time Factors; D014357:Trypsin / Q000737:chemistry
chemical_list: D004151:Dipeptides; D015842:Serine Proteinase Inhibitors; C104090:arginyllysine; C076685:arginylarginine; D012697:Serine Endopeptidases; D014357:Trypsin