Comparison of the multicatalytic proteinases isolated from the nucleus and cytoplasm of chicken red blood cells.
1. Two chromatographically distinct multicatalytic proteinases (MCP's) were isolated from the cytoplasm of chicken red blood cells and one MCP was purified from the nuclei. 2. The nuclear and the majority (97-99%) of the cytoplasmic multicatalytic proteolytic activity were chromatographically similar and differed from the minor cytoplasmic activity in their elution from hydroxylapatite, number of subunits on 2D-SDS-PAGE, and in their sensitivity to proteinase inhibitors. 3. Dichloroisocoumarin, a serine proteinase inhibitor, inhibited the hydrolysis of fluorogenic peptides but stimulated the degradation of casein by the multicatalytic proteinases suggesting that this enzyme has distinct active sites for protein and peptide hydrolysis.
Strack
P R
PR
Department of Animal Sciences, Rutgers University, New Brunswick, NJ 08903.
Wajnberg
E F
EF
Waxman
L
L
Fagan
J M
JM
D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology*; D002645:Chickens; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D003546:Cysteine Endopeptidases / Q000187:drug effects / Q000302:isolation & purification / Q000378:metabolism*; D003593:Cytoplasm / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000201:enzymology*; D007526:Isoelectric Point; D008297:Male; D009097:Multienzyme Complexes / Q000187:drug effects / Q000302:isolation & purification / Q000378:metabolism*; D011107:Polylysine / Q000494:pharmacology; D046988:Proteasome Endopeptidase Complex
D009097:Multienzyme Complexes; D011107:Polylysine; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex