Purification of biotin-binding protein from chicken egg yolk and comparison with avidin

Ramana Murthy, C. V. ; Adiga, P. Radhakantha (1984) Purification of biotin-binding protein from chicken egg yolk and comparison with avidin Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology, 786 (3). pp. 222-230. ISSN 0167-4838

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/016748...

Related URL: http://dx.doi.org/10.1016/0167-4838(84)90092-X


A simple alternative procedure for the purification in higher yields of the biotin-binding protein from the chicken egg yolk in a ligand-free form is described. The isolated protein was homogenous by the criteria of polyacrylamide gel electrophoresis, gel filtration chromatography, immuno-double diffusion and immunoelectrophoresis. The protein had an Mr of 72000 ± 2000 and was a homotetramer of subunit Mr of 18000 ±1000. It bound [14C]biotin in the molar ratio of 1:4 with an association constant (Ka) of 0.58 1012M-1. The yolk biotin-binding protein and avidin exhibited qaulitatively similar spectral changes on interaction with biotin and p-hydroxyazobenzoic acid, but quantitatively these changes were more pronounced with avidin. Despite the lack of gross immunological cross-reactivity between the two biotin-binders, evidence based on immunological techniques for some degree of common conformational characteristics restricted to or around the ligand-binding sites of the two proteins was adduced. The mixed subunits of the two proteins failed to form hetero-oligomers on reconstitution.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Biotin-binding Protein; Subunit Composition; Ligand Binding; Avidin; (Chicken Egg Yolk)
ID Code:26825
Deposited On:08 Dec 2010 13:07
Last Modified:13 May 2011 04:55

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