Characterisation and partial purification of a novel prohormone processing enzyme from ovine adrenal medulla.
An enzymatic activity has been identified which is capable of generating a product chromatographically identical with adrenorphin from the model substrate BAM12P. This enzyme was purified by gel filtration and ion-exchange chromatography and characterised as having a molecular mass between 30 and 45 kDa and an acidic pI. The enzyme is active at the acid pH expected in the secretory vesicle interior and is inhibited by EDTA, suggesting that it is a metalloprotease. This activity could not be mimicked by incubation with lysosomal fractions and it meets the criteria to be considered as a possible prohormone processing enzyme.
Tezapsidis
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Biochemistry Group, School of Biological Sciences, University of Sussex, Brighton, England.
Parish
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D000313:Adrenal Medulla / Q000201:enzymology* / Q000648:ultrastructure; D000818:Animals; D002458:Cell Fractionation; D002499:Centrifugation, Density Gradient; D002837:Chromaffin Granules / Q000201:enzymology; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004229:Dithiothreitol / Q000494:pharmacology; D004492:Edetic Acid / Q000494:pharmacology; D010450:Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D004744:Enkephalin, Methionine / Q000031:analogs & derivatives* / Q000378:metabolism; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism; D008970:Molecular Weight; D011480:Protease Inhibitors / Q000494:pharmacology; D011498:Protein Precursors / Q000378:metabolism*; D012756:Sheep
D011480:Protease Inhibitors; D011498:Protein Precursors; D004744:Enkephalin, Methionine; C026771:BAM 12P; C039700:adrenorphin; D004492:Edetic Acid; D010450:Endopeptidases; D008666:Metalloendopeptidases; D004229:Dithiothreitol