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An amphibian two‐domain ‘big’ neurophysin: conformational homology with the mammalian MSEL‐neurophysin/copeptin intermediate precursor shown by trypsin‐Sepharose proteolysis
Author(s) -
Chauvet Jacqueline,
Michel Gilles,
Chauvet Marie-Thérèse,
Acher Roger
Publication year - 1988
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(88)80645-8
Subject(s) - neurophysins , proteolysis , trypsin , biochemistry , vasotocin , chemistry , biology , sepharose , enzyme , neuropeptide , hormone , receptor
A ‘big’ frog ( Rana esculenta ) neurophysin, encompassing sequences homologous to mammalian MSEL‐neurophysin and copeptin, has been passed through a trypsin‐Sepharose column in order to compare its conformation with that of the two‐domain intermediate precursor isolated from guinea pig. Whereas the polypeptide possesses 8 arginine residues, only two cleavages were observed located in a putative inter‐domain sequence (at Arg‐94 and Arg‐114). Because free vasotocin has been isolated from the frog, it is assumed that pro‐vasotocin has a three‐domain conformation similar to that of pro‐vasopressin but processing in amphibians involves only one step rather than two steps as in mammals.