Chromogranin A-processing proteinases in purified chromaffin granules: contaminants or endogenous enzymes?

• Published in: Biochimica et biophysica acta Vol. 1033; no. 1; pp. 65 - 72
• Main Authors: Laslop, Andrea, Fischer-Colbrie, Reiner, Kirschke, Heidrun, Hogue-Angeletti, Ruth, Winkler, Hans
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 29.01.1990; Elsevier; North-Holland
• Subjects: 4-Chloromercuribenzenesulfonate - pharmacology; Adrenal Medulla - ultrastructure; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Calcium - pharmacology; Cathepsin B - isolation & purification; Cathepsin B - metabolism; Cathepsin D - isolation & purification; Cathepsin D - metabolism; Cattle; Chromaffin granule; Chromaffin Granules - enzymology; Chromaffin System - enzymology; Chromatography; Chromogranin A; Chromogranins - metabolism; Cysteine Endopeptidases - analysis; Cysteine Endopeptidases - metabolism; Electrophoresis, Polyacrylamide Gel; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Hydrogen-Ion Concentration; Hydrolases; Immunoblotting; Lysosomes - enzymology; Nerve Tissue Proteins - metabolism; Pepstatins - pharmacology; Peptide Hydrolases - analysis; Peptide Hydrolases - metabolism; Protease Inhibitors; Proteinase; Trypsin - analysis; Trypsin - metabolism; Chromogranin A; PCMPS; Chromaffin granule; Proteinase; Bovine; Gel electrophoresis; Enzyme; Adrenal medulla; HPLC chromatography; Proteins; Substrate; Vertebrata; Mammalia; Chromogranin; Enzymatic activity; Affinity chromatography; Blotting assay; Substrate specificity; Gel filtration; Artiodactyla; Ungulata

It was the purpose of this study to define the chromogranin A-processing proteinases present in highly purified preparations of bovine chromaffin granules. The most active enzyme had a pH optimum of 5.0 and was inhibited by pepstatin. It could be identified immunologically as a cathepsin D-like enzy...