Purification and characterization of a proteinase inhibitor from white croaker skeletal muscle ( Micropogon opercularis)

A trypsin proteinase inhibitor has been purified to homogeneity from the skeletal muscle of white croaker ( Micropogon opercularis). Previously, we had described the occurrence in fish muscle of a serine protease (proteinase I) which showed a great capacity to degrade whole myofibrils in vitro and a...

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Veröffentlicht in:	The international journal of biochemistry & cell biology 2001-07, Vol.33 (7), p.691-699
Hauptverfasser:	Sangorrı́n, M.P, Folco, E.J, Martone, C.M, Sánchez, J.J
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Caseins - metabolism Chromatography, Gel Electrophoresis, Polyacrylamide Gel Fish muscle Hydrogen-Ion Concentration Molecular Weight Muscle protein breakdown Muscle, Skeletal - chemistry Muscle, Skeletal - enzymology Myofibrils Perciformes - metabolism Proteolysis Serine Endopeptidases - metabolism Serine Proteinase Inhibitors - chemistry Serine Proteinase Inhibitors - isolation & purification Serine Proteinase Inhibitors - pharmacology Temperature Trypsin inhibitor Trypsin Inhibitors - chemistry Trypsin Inhibitors - isolation & purification Trypsin Inhibitors - pharmacology
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