| Autor: |
Blagrove, RJ, Lilley, GG, Higgins, TJV |
| Zdroj: |
Australian Journal of Plant Physiology; 1984, Vol. 11 Issue: 2 p69-77, 9p |
| Abstrakt: |
The isolation, characterization and amino acid composition are reported for macrozin, the major storage globulin found in seeds of Macrozamia communis. Electrophoresis of macrozin on cellulose acetate membranes at neutral pH resulted in a single broad band indicating limited charge heterogeneity. Isoelectric focusing under dissociating and reducing conditions showed this globulin to be composed of a family of polypeptide chains with apparent isoelectric points in the range pH 6.0-7.5. Sedimentation equilibrium studies showed that the main component purified by gel filtration in aqueous buffers at neutral pH has a molecular weight of 260 000 and a sedimentation coefficient S020.w = 10.9 S. This component dissociates in 8 M urea to yield subunits of molecular weight 126 000. Each subunit is composed of disulfide-bonded polypeptide chains of approximate molecular weight 44 000. The apparent molecular weights for the macrozin subunit and its constituent polypeptides were 130 000 and 46 000 from dodecyl sulfate-polyacrylamide gradient gel electrophoresis. The dimeric nature of the main oligomer in aqueous solution was confirmed by crosslinking the subunits with dithiobis(succinimidylpropionate); the presence of three polypeptide chains per subunit is inferred from the molecular weights. Optical rotatory dispersion and circular dichroism measurements suggest that macrozin is devoid of α-helix in its native conformation, but contains some 25% α-helix after incubation with sodium dodecyl sulfate. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
