Salunke, DM and Khan, Islam M and Surolia, A and Vijayan, M (1983) Preparation and preliminary x-ray studies of three acidic pH crystal forms of the anti-T lectin from peanut (Arachis hypogaea). In: FEBS Letters, 156 (1). pp. 127-129.
Restricted to Registered users only
Download (260Kb) | Request a copy
Lectins, by definition, are multivalent carbohydrate binding proteins. Their earlier generic name 'phytohaemagglutinins' arose from their ability to agglutinate erythrocytes and from the fact that, until recently, all the described lectins were from plant sources [l]. These proteins have been subsequently found in many animal species and probably they occur in all forms of life . The interesting properties of lectins arise from their ability to bind specific cell-surface carbohydrates. Lectins have assumed considerable importance in recent years on account of their potential for use in studies on biological receptors and cell-surface phenomena.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Elsevier Science|
|Keywords:||Peanut lectin;New crystal form;X-ray analysis|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||10 Apr 2008|
|Last Modified:||19 Sep 2010 04:44|
Actions (login required)