N2404
Neurophysin I from bovine pituitary
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About This Item
Form
solid
Mol-Gew.
~10 kDa
Lagertemp.
2-8°C
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Biochem./physiol. Wirkung
Mutations leading to disruptions of the structure and/or conformation of neurophysins are implicated in the pathophysiology of central diabetes insipidus (CDI).
Sonstige Hinweise
Protein found in vasopressin- and oxytocin-containing neurons in the hypothalamus that is associated with the transport of these hormones to the posterior pituitary.
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves, type N95 (US)
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Highly purified neurophysin proteins: method of isolation based on their acidic properties.
T K Audhya et al.
Archives of biochemistry and biophysics, 180(1), 130-139 (1977-04-15)
R Kaźmierkiewicz et al.
Acta biochimica Polonica, 44(3), 453-466 (1997-01-01)
This is a review of our recent modeling work aimed at: (i) development and assessment of techniques for reliable refinement of low-resolution protein structures and (ii) using these techniques, at solving specific problems pertinent to neurophysin-bioligand interactions. Neurophysins I and
J K Kim et al.
Proceedings of the Association of American Physicians, 110(5), 380-386 (1998-10-02)
The arginine vasopressin (AVP) precursor gene of mammals contains three exons encoding the principal domains of the polyprotein precursor, including vasopressin (exon A), neurophysin (exon B), and glycopeptide (exon C). The AVP precursor (preprohormone) is processed and transported through the
J J Legros et al.
Hormone research, 45(3-5), 182-186 (1996-01-01)
When they were discovered by Acher and co-workers, neurophysins were thought to act as carriers for the active nonapeptides vasopressin (AVP) and oxytocin (OT) and were then recognized as the inactive fragment of a precursor with a higher molecular weight
F M de Bree et al.
Cellular and molecular neurobiology, 18(2), 173-191 (1998-04-16)
1. In this review the structure-function relationships of the different vasopressin prohormone domains are dated and discussed, with special reference to the neurophysin and glycopeptide domains. 2. The primary structures of the currently known neurophysins and glycopeptide sequences are compared
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