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The presence of an endopeptidase hydrolyzing succinyl trialanine-p-nitroanilide [Suc(Ala)3-pNA] to Suc(Ala)2 and Ala-pNA in human kidney and its partial characterization have been reported (Ishida et al. (1981) Biochem. Int. 3, 239-246). This neutral metallo-endopeptidase was separated into two fractions (A and B) on Sephacryl S-300 and fraction B was further purified to an electrophoretically pure state. The fraction B enzyme had a molecular weight of 100,000 and was inhibited by metal chelators such as EDTA, o-phenanthroline and phosphoramidon, but not by serine protease inhibitors. The enzyme was found to hydrolyze peptide bonds preferentially at the amino sides of hydrophobic amino acids such as Leu and Phe, when its specificity was studied using insulin B chain and angiotensin I. Fraction A seems to be a tetramer of fraction B, judging from its molecular weight, pI, substrate specificity and immunological properties.
M Ishida, and
M Ogawa, and
G Kosaki, and
T Mega, and
T Ikenaka
February 1987,
Biochemical medicine and metabolic biology,
M Ishida, and
M Ogawa, and
G Kosaki, and
T Mega, and
T Ikenaka
December 1998,
Journal of hypertension,
M Ishida, and
M Ogawa, and
G Kosaki, and
T Mega, and
T Ikenaka
March 1974,
The Biochemical journal,
M Ishida, and
M Ogawa, and
G Kosaki, and
T Mega, and
T Ikenaka
June 1985,
Biochimica et biophysica acta,
M Ishida, and
M Ogawa, and
G Kosaki, and
T Mega, and
T Ikenaka
October 1987,
Archives of biochemistry and biophysics,
M Ishida, and
M Ogawa, and
G Kosaki, and
T Mega, and
T Ikenaka
June 1984,
Biochimica et biophysica acta,
M Ishida, and
M Ogawa, and
G Kosaki, and
T Mega, and
T Ikenaka
June 1984,
Journal of biochemistry,
M Ishida, and
M Ogawa, and
G Kosaki, and
T Mega, and
T Ikenaka
May 1994,
Archives of biochemistry and biophysics,
M Ishida, and
M Ogawa, and
G Kosaki, and
T Mega, and
T Ikenaka
May 1991,
The Biochemical journal,
M Ishida, and
M Ogawa, and
G Kosaki, and
T Mega, and
T Ikenaka
September 1991,
European journal of biochemistry,
