Structure and properties of ovalbumin

被引：285

作者：

Huntington, JA ^{[1
]}

Stein, PE ^{[1
]}

机构：

[1] Univ Cambridge, Dept Haematol, Wellcome Trust Ctr Mol Mech Dis, Cambridge Inst Med Res, Cambridge CB2 2XY, England

来源：

JOURNAL OF CHROMATOGRAPHY B | 2001年 / 756卷 / 1-2期

关键词：

food allergy; ovalbumin;

D O I：

10.1016/S0378-4347(01)00108-6

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Ovalbumin is a protein of unknown function found in large quantities in avian egg-white. Surprisingly, ovalbumin belongs to the serpin family although it lacks any protease inhibitory activity. We review here what is known about the amino acid sequence, post-translational modifications and tertiary structure of ovalbumin. The properties of ovalbumin are discussed in relation to their possible functional significance. These include reasons for failure of ovalbumin to undergo a typical serpin conformational change involving the reactive centre loop, which explains why ovalbumin is not a protease inhibitor, and also the natural conversion of ovalbumin to the more stable "S" form. (C) 2001 Elsevier Science B.V. All rights reserved.

引用

页码：189 / 198

页数：10

共 71 条

[1] Structural properties of recombinant ovalbumin and its transformation into a thermostabilized form by alkaline treatment [J].