title: Identification of four distinct serine proteinase inhibitors in rat skeletal muscle.
abstract: The serine proteinase inhibitory capacity in the cytosolic fraction of rat skeletal muscle tissue is accounted for by several discrete inhibitory activities. Three of these activities are identical with the proteinase inhibitors alpha 1-proteinase inhibitor, rat proteinase inhibitor I and rat proteinase inhibitor I I respectively, which have been recently characterized as major serine proteinase inhibitors in rat serum (Kuehn, L., Rutschmann, M., Dahlmann, B. and Reinauer, H. (1984) Biochem. J. 218, in the press). The other inhibitor molecule, having an Mr of about 15 000, appears to be an endogenous inhibitor.
mesh_terms: D000818:Animals; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D003600:Cytosol / Q000378:metabolism; D005779:Immunodiffusion; D008297:Male; D009132:Muscles / Q000378:metabolism*; D011480:Protease Inhibitors / Q000302:isolation & purification*; D011506:Proteins / Q000302:isolation & purification*; D051381:Rats; D011919:Rats, Inbred Strains; D015842:Serine Proteinase Inhibitors
chemical_list: D011480:Protease Inhibitors; D011506:Proteins; D015842:Serine Proteinase Inhibitors