Characterisation and partial purification of a novel prohormone processing enzyme from ovine adrenal medulla

FEBS Letters

Tezapsidis, N.¹  Parish, D.C.¹ 

[1] Biochemistry Group, School of Biological Sciences, University of Sussex, Falmer, Brighton, Sussex, England

关键词: Prohormone processing;    Adrenorphin;    Secretory vesicle purification;    BAM12P;    bovine adrenal medullary dodecapeptide;    HPLC;    high-pressure liquid chromatography;    Mes;    morpholinoethanosulphonic acid;    PAM;    peptidyl-glycine α-amidating mono-oxygenase;   

DOI  :  10.1016/0014-5793(89)80250-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 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.

【 授权许可】

Unknown