تفاصيل الوثيقة

نوع الوثيقة : مقال في مجلة دورية 
عنوان الوثيقة :
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
 
الموضوع : كيمياء حيوية 
لغة الوثيقة : العربية 
المستخلص : 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. 
ردمد : 1093-2607 
اسم الدورية : Human Antibodies, Volume 17, Issue 3-4, 2008, Pages 85-96 
المجلد : 17 
العدد : 3 
سنة النشر : 2008 هـ
2008 م 
عدد الصفحات : 11 
نوع المقالة : مقالة علمية 
تاريخ الاضافة على الموقع : Thursday, October 15, 2009 

الباحثون

اسم الباحث (عربي)اسم الباحث (انجليزي)نوع الباحثالمرتبة العلميةالبريد الالكتروني
سوسن حسان محمدشوكت محاسنيSawsan Hassan Mahassniباحثدكتوراهsmahasni@kau.edu.sa
Klapper, D.GKlapper, D.Gباحثدكتوراه 
Hiskey, R.GHiskey, R.Gباحثدكتوراه 

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