title: Purification and characterization of an inhibitor of the cysteine protease from the hemolymph of Sarcophaga peregrina larvae.
abstract: The hemolymph of Sarcophaga peregrina (flesh fly) larvae was found to contain multiple inhibitors of hemocyte cysteine protease. One of them, named sarcocystatin A, was purified and found to be a mixture of the components sarcocystatin A alpha and A beta in a molar ratio of 2:1. These components can exist in either the associated or dissociated form. The apparent heterogeneity of the protease inhibitors in the hemolymph was found to be partly due to association of sarcocystatin A alpha and A beta.
mesh_terms: D000818:Animals; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003546:Cysteine Endopeptidases; D015853:Cysteine Proteinase Inhibitors; D004175:Diptera; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism*; D006458:Hemolymph / Q000032:analysis*; D006863:Hydrogen-Ion Concentration; D007814:Larva / Q000201:enzymology; D010446:Peptide Fragments / Q000032:analysis; D011480:Protease Inhibitors / Q000302:isolation & purification*; D011506:Proteins / Q000032:analysis*; D014357:Trypsin / Q000378:metabolism
chemical_list: D015853:Cysteine Proteinase Inhibitors; D010446:Peptide Fragments; D011480:Protease Inhibitors; D011506:Proteins; D010450:Endopeptidases; D014357:Trypsin; D003546:Cysteine Endopeptidases