One-step processing of the amphibian vasotocin precursor: Structure of a frog ( Rana esculenta) “big” neurophysin
Vasotocin-associated neurophysin (MSEL-neurophysin) from the frog Rana esculenta has been isolated and sequenced through tryptic and staphylococal proteinase peptides and cyanogen bromide fragments. This protein appears homologous to the mammalian vasopressin-associated neurophysin with a C-terminal...
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Veröffentlicht in: | Biochemical and biophysical research communications 1987-12, Vol.149 (2), p.538-544 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Vasotocin-associated neurophysin (MSEL-neurophysin) from the frog
Rana esculenta has been isolated and sequenced through tryptic and staphylococal proteinase peptides and cyanogen bromide fragments. This protein appears homologous to the mammalian vasopressin-associated neurophysin with a C-terminal glycopeptide extension homologous to the mammalian copeptin. In contrast to the two-step processing of mammalian vasopressin/MSEL-neurophysin/copeptin precursor, a single cleavage is therefore involved in the processing of the amphibian vasotocin/neurophysin precursor. It appears that the physiological release of the vasopressin-like hormone from the N-terminal end of the protein precursor is not dependent upon a previous trimming of the C-terminal copeptin-like moiety. |
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ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/0006-291X(87)90401-3 |