Conformation limited proteolysis in the common neurophysin‐copeptin precursor shown by trypsin‐Sepharose chromatographic proteolysis

FEBS Letters

Chauvet, Jacqueline¹  Chauvet, Marie-Thérèse¹  Acher, Roger¹ 

[1] Laboratory of Biological Chemistry, University of Paris VI, 96, Boulevard Raspail, 75006 Paris, France

关键词: Neurophysin-copeptin precursor;    Prohormone processing enzyme;    Conformation-limited proteolysis;    Enzyme specificity;    Affinity chromatography;   

DOI  :  10.1016/0014-5793(87)80659-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The guinea pig two-domain precursor of MSEL-neurophysin and copeptin has been passed through a trypsin-Sepharose column in order to mimic the enzyme processing by a membrane-bound endopeptidase. Only two cleavages were observed located in the inter-domain sequence (at Arg-94 and Arg-98), in contrast to several additional cleavages found when free neurophysin or copeptin is subjected to soluble trypsin. Because the physiological maturation involves a single cleavage at Arg-94, both local accessibility in the precursor and narrow specificity of the enzyme are implied in the processing.

【 授权许可】

Unknown