Further characterization of a sarcoplasmic serine proteinase from the skeletal muscle of white croaker (Argyrosomus argentatus).
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.
Cao
Min-Jie
MJ
College of Biological Engineering, Jimei University, Jimei, Xiamen, 361021, China. mjcao@jmu.edu.cn
Hara
Kenji
K
Weng
Ling
L
Zhang
Nong
N
Su
Wen-Jin
WJ
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
D004151:Dipeptides; D015842:Serine Proteinase Inhibitors; C104090:arginyllysine; C076685:arginylarginine; D012697:Serine Endopeptidases; D014357:Trypsin