A Succinyl-Trialanine P-Nitroanilide Hydrolase in Hog Kidney Cytosol: Its Identification as Proline Endopeptidase.

Chemical and Pharmaceutical Bulletin- Japan

doi 10.1248/cpb.32.1510

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Date

January 1, 1984

Authors

SHINJI SOEDA

MASANORI OHYAMA

ATSUO NAGAMATSU

Publisher

Pharmaceutical Society of Japan

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A Succinyl-Trialanine P-Nitroanilide Hydrolase in Hog Kidney Cytosol: Its Identification as Proline Endopeptidase.

Chemical and Pharmaceutical Bulletin- Japan

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

Partial Purification of the Enzyme Obtained From the Rat Kidney Microsomal Membrane With Succinyl Trialanine P-Nitroanilide-Hydrolyzing Activity and the One Similar to Signal Peptidase.

Bacteria of the Genus Bacillus Have a Hydrolase Stereospecific to the D Isomer of Benzoyl-Arginine-P-Nitroanilide.

The Synthesis of Benzoyl-L-Arginine-P-Nitroanilide

Proteins of the Kidney Microvillar Membrane. Purification and Properties of the Phosphoramidon-Insensitive Endopeptidase (‘Endopeptidase-2’) From Rat Kidney

A Novel Synthesis of L-Pyroglutamyl-Glycyl-L-Arginine-P-Nitroanilide Hydrochloride.

Pig Kidney Legumain: An Asparaginyl Endopeptidase With Restricted Specificity

Identification of Α,β-Hydrolase Domain Containing Protein 6 as a Diacylglycerol Lipase in Neuro-2a Cells

Intermediate Molecular Weight Renin and Renin-Binding Protein(s) in the Hog Kidney

Characterization of PHEX Endopeptidase Catalytic Activity: Identification of Parathyroid-Hormone-Related Peptide107–139 as a Substrate and Osteocalcin, PPi and Phosphate as Inhibitors