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Characterisation and partial purification of a novel prohormone processing enzyme from ovine adrenal medulla
Author(s) -
Tezapsidis N.,
Parish D.C.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80250-9
Subject(s) - prohormone , enzyme , size exclusion chromatography , biochemistry , adrenal medulla , chemistry , chromatography , substrate (aquarium) , enzyme assay , molecular mass , incubation , ion chromatography , biology , hormone , endocrinology , ecology , catecholamine
An enzymatic activity has been identified which is capable of generating a product chromatographically identical with adrenorphin from the model substrate BAM 12P. 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 p I . 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.