Document Details

Document Type : Article In Journal 
Document Title :
Production of metal ion-dependent monoclonal antibodies against peptides in bovine prothrombin fragment 1
Production of metal ion-dependent monoclonal antibodies against peptides in bovine prothrombin fragment 1
 
Subject : Biochemistry 
Document Language : Arabic 
Abstract : Bovine prothrombin fragment 1 (F-1: the amino-terminal 156 residues of prothrombin) is used as a model to study the Ca(II) and phospholipid binding of prothrombin. The 35-46 segment in F-1 posses an α-helical region and three aromatic residues, conserved in several vitamin K-dependent blood coagulation factors. These residues are believed to have a specific function and to be important in the phospholipid binding of F-1. The 47-62 region, a disulfide loop, is believed to stabilize the γ-carboxyglutamic acid domain of the protein. Goals of this research were to produce monoclonal antibodies against the above two sequences, for later functional studies. Antibodies S9-32.8 and S9-5.5 were produced against the 35-46 sequence; antibody S11-23.4 was raised against the 47-62 region. Both S9-32.8 and S9-5.5 bound to F-1 immobilized on ELISA plates in the presence of 10 mM Ca(II) with higher affinity than to F-1 coated in the presence of 10 mM Mg(II) or in the absence of metal ions. S11-23.4 showed greatest binding to F-1 coated in the presence of 10 mM Mg(II). Thus, the epitopes of the antibodies are metal ion-dependent and are developed by Ca(II) binding to F-1. © 2008 - IOS Press and the authors. All rights reserved. 
ISSN : 1093-2607 
Journal Name : Human Antibodies, Volume 17, Issue 3-4, 2008, Pages 85-96 
Volume : 17 
Issue Number : 3 
Publishing Year : 2008 AH
2008 AD 
Number Of Pages : 11 
Article Type : Article 
Added Date : Thursday, October 15, 2009 

Researchers

Researcher Name (Arabic)Researcher Name (English)Researcher TypeDr GradeEmail
سوسن حسان محمدشوكت محاسنيSawsan Hassan MahassniResearcherDoctoratesmahasni@kau.edu.sa
Klapper, D.GKlapper, D.GResearcherDoctorate 
Hiskey, R.GHiskey, R.GResearcherDoctorate 

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