Sreekrishna, K and Cama, HR (1979) Characterization of vitamin A transport system from goat plasma. In: Biochimica et Biophysica Acta (BBA) - Protein Structure, 581 (1). pp. 136-141.
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Retinol-binding protein and its complex with prealbumin were isolated from goat serum by chromatography on DEAE-Sephadex A-50, gel filtration and immuno-affinity chromatography on antigoat-serum albumin-Sepharose 4B. The homogeneous prealbumin-retinol-binding protein complex had a molecular weight of 75 000. Both on electrophoresis and in the presence of 2 M urea, the complex dissociated into retinol-binding protein and prealbumin. The molecular weight, electrophoretic behaviour, ultraviolet and fluorescence spectra of goat retinol-binding protein were similar to those isolated from other sources. On sodium dodecyl sulphate gel electrophoresis, goat prealbumin (molecular weight ≈ 55 000) exhibited two bands corresponding to molecular weights 26 000 and 13 000. This suggests that either goat prealbumin consists of two non-identical sub-units or perhaps complete dissociation might not have occurred. Goat prealbumin was able to bind Image -thyroxine and retinol-binding protein.
|Item Type:||Journal Article|
|Additional Information:||Copy right of this article belongs to Elsevier Science.|
|Department/Centre:||Division of Biological Sciences > Biochemistry|
|Date Deposited:||27 Oct 2009 13:40|
|Last Modified:||19 Sep 2010 05:49|
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