We have used gel-filtration chromatography on columns of "Ultragel" in 1.0 M sodium chloride to fractionate the soluble proteins of the yolkof Australorp hen's eggs. Five fractions were isolated quantitatively: three major fractions each about a third of the total soluble protein by weight and each
Structural studies of the hen's egg lipovitellins. NMR and fluorescence investigations
β Scribed by D.N. Ramakrishna Rao; S. Mahadevan; P. Balaram
- Publisher
- Elsevier Science
- Year
- 1978
- Tongue
- English
- Weight
- 408 KB
- Volume
- 22
- Category
- Article
- ISSN
- 0009-3084
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β¦ Synopsis
The pH dependent reversible association-dissociation reaction of co-and fl-lipoviteUins from egg yolk has been studied by IH NMR and fluorescence probe methods. Increased mobility of the choline methyl groups has been demonstrated on dissociation. The lipid methylene resonance of 0-lipovitellin shows clear doublet character suggesting that the fatty acid chains exist in distinct environments. The high field component increases with temperature but is suppressed on treatment with pronase, suggesting a significant role for proteins in maintaining the differences in lipid environments. 1-Anilino-8-naphthalene sulfonate has been shown to bind less effectively to the monomeric lipovitellins. This is in agreement with earlier results suggesting that dissociation may be accompanied by increased hydration and conformational changes.
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