Isolation and characterization of a neurophysin from ostrich neurohypophyses
| Autor: | Ryno J. Naudé, Willem Oelofsen, Hesta S. Saayman |
|---|---|
| Rok vydání: | 1985 |
| Předmět: |
Fractionation
Biochemistry High-performance liquid chromatography Birds chemistry.chemical_compound Residue (chemistry) Pituitary Gland Posterior Animals Amino Acid Sequence Cyanogen Bromide Amino Acids Chromatography High Pressure Liquid chemistry.chemical_classification Neurophysins Chromatography Isoelectric focusing Chromatography Ion Exchange Peptide Fragments Amino acid Molecular Weight chemistry Sephadex Chromatography Gel Cyanogen bromide Electrophoresis Polyacrylamide Gel Ultracentrifuge Isoelectric Focusing hormones hormone substitutes and hormone antagonists |
| Zdroj: | International journal of peptide and protein research. 26(4) |
| ISSN: | 0367-8377 |
| Popis: | A neurophysin has been isolated from ostrich neurohypophyses using acid acetone extraction, salt fractionation and Sephadex G-75 chromatography. The crude neurophysin eluting from the Sephadex G-75 column was subjected to a) reverse-phase HPLC followed by Sephadex G-75 chromatography, b) DEAE-Sephadex A-50 chromatography or c) isoelectric focusing. The different homogeneous ostrich neurophysin fractions so obtained were compared i.t.o. amino acid composition, spectral properties, N-terminal amino acid residues and PAGE. They all revealed a single N-terminal Ala residue and displayed spectral properties (A280/A260 less than 1) which are typical of mammalian neurophysin-like polypeptides. Ultracentrifugation studies on purified ostrich neurophysin over a range of concentrations revealed a reversible concentration dependent association behaviour characterized by the presence of dimeric complexes at higher concentrations. Partial sequencing from the N-terminus revealed the molecule to be VLDV-like. The purified molecule was also submitted to CNBr fragmentation. |
| Databáze: | OpenAIRE |
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