TY - JOUR
T1 - A putative prohormone processing protease in bovine adrenal medulla specifically cleaving in between Lys-Arg sequences
AU - Mizuno, Kensaku
AU - Kojima, Masayasu
AU - Matsuo, Hisayuki
N1 - Funding Information:
We thank Dr. K. Takada for his kind supply of Boc-Leu-Lys-Arg-MCA, Dr. K. Kangawa for his valuable comments and Mrs. T. Hatoh and R. Nishi for technical assistance. This investigation was supported in part by research grant from the Ministry of Education, Science and Culture of Japan.
PY - 1985/4/30
Y1 - 1985/4/30
N2 - Paired basic residues, particularly Lys-Arg, are known as a typical site for proteolytic processing of prohormones. In this study, we confirmed the presence of a novel protease exhibiting substrate specificity toward Lys-Arg sequence. It was partially purified from the soluble fraction of bovine adrenomedullary chromaffin granules by using an affinity chromatography on soybean trypsin inhibitor-Sepharose. The enzyme, with optimal pH around 7.5-9.5, is classified into a serine-protease family by its inhibition spectrum. The enzyme specifically cleaves in between the Lys-Arg bonds of the peptides related to proenkephalins, but the sequences of Arg-Arg, Arg-Lys and a single basic residue (Arg or Lys) in the substrates are not affected by the enzyme. The unique substrate specificity of the enzyme suggests that it is distinct from pancreatic trypsin and may be physiologically involved in proenkephalin processing.
AB - Paired basic residues, particularly Lys-Arg, are known as a typical site for proteolytic processing of prohormones. In this study, we confirmed the presence of a novel protease exhibiting substrate specificity toward Lys-Arg sequence. It was partially purified from the soluble fraction of bovine adrenomedullary chromaffin granules by using an affinity chromatography on soybean trypsin inhibitor-Sepharose. The enzyme, with optimal pH around 7.5-9.5, is classified into a serine-protease family by its inhibition spectrum. The enzyme specifically cleaves in between the Lys-Arg bonds of the peptides related to proenkephalins, but the sequences of Arg-Arg, Arg-Lys and a single basic residue (Arg or Lys) in the substrates are not affected by the enzyme. The unique substrate specificity of the enzyme suggests that it is distinct from pancreatic trypsin and may be physiologically involved in proenkephalin processing.
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U2 - 10.1016/0006-291X(85)90129-9
DO - 10.1016/0006-291X(85)90129-9
M3 - Article
C2 - 3922369
AN - SCOPUS:0021834950
VL - 128
SP - 884
EP - 891
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -