Specific cleavages of arginyl peptide bonds at basic amino acid pairs by a serine proteinase from the microsomal membranes of rat liver.
The specificity of action of a serine proteinase from the microsomal membranes of rat liver was investigated at pH 7.5 and 37 degrees C using various peptides as substrates. HPLC analyses of the peptides produced followed by their amino acid analyses have revealed that the enzyme is a unique endopeptidase specifically cleaving arginyl peptide bonds at paired basic amino acid residues. Thus, the enzyme is suggested to be a kind of processing proteinase involved in the conversion of proproteins to their mature forms. Indeed, the enzyme cleaved specifically the NH2-terminal 20-residue peptide of proalbumin at the Arg-Arg sequence.
Takahashi
K
K
Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Japan.
Tamanoue
Y
Y
Yanagida
M
M
Sakurai
Y
Y
Takahashi
T
T
Sutoh
K
K
D000595:Amino Acid Sequence; D000818:Animals; D001120:Arginine; D002851:Chromatography, High Pressure Liquid; D007425:Intracellular Membranes / Q000201:enzymology*; D008862:Microsomes, Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D051381:Rats; D012697:Serine Endopeptidases / Q000378:metabolism*; D013379:Substrate Specificity
D010446:Peptide Fragments; D001120:Arginine; D012697:Serine Endopeptidases