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Vol.40 No.6 >

Please use this identifier to cite or link to this item: http://hdl.handle.net/10564/2104

Title: Ristocetin血小板凝集を抑制する抗von Willebrand因子モノクローナル抗体の多様性
Other Titles: HETEROGENEITY OF ANTI-VON WILLEBRAND FACTOR (VWF) ANTIBODIES WHICH INHIBIT RISTOCETIN-INDUCED VWF BINDING TO PLATELET GLYCOPROTEIN (GP)Ⅰb
Authors: 新家, 興
西尾, 健治
中井, 寛明
嶋, 緑倫
高瀬, 俊夫
金田, 美喜夫
吉岡, 章
福井, 弘
藤村, 吉博
Keywords: von Willebrand factor
monoclonal antibody
epitope
ristocetin
botrocetin
Issue Date: 31-Dec-1989
Publisher: 奈良医学会
Citation: 奈良医学雑誌 Vol.40 No.6 p.797-801
Abstract: The epitopes of four anti-vWF monoclonal antibodies (MoAbs), which inhibit antibiotic ristocetin induced vWF binding to GPⅠb, were investigated and compared with each other. MoAb NMC-4 completely inhibited both the vWF bindings to GPⅠb expressed by ristocetin and snake venom botrocetin at the final concentrations of 10 μg/ml. Another MoAb RFF-VⅢ RAG : 1 also completely inhibited ristocetin-induced vWF binding at the IgG concentration of 10 μg/ml, but showed a partial inhibition (75% at the IgG concentlation of 100 μg/ml) on botrocetin-induced binding. Two other MoAbs, RG46 and 52-K8, inhibited ristocetin-induced vWF binding at the inhibition constant by 50% of 90 μg/ml and 30 μg/ml respectively, but without effect on botrocetin-induced vWF binding. Using the radiolabelled NMC-4 and its binding to vWF immobilized to plastic tubes, the competitive binding assay was performed. In this assay, cold NMC-4 clearly displaced (¹²⁵Ⅰ) NMC-4 binding to solid-phase vWF, and RFF-VⅢRAG : 1 partially blocked the binding (60% at the IgG concentration of 100 μg/ml), whereas neither RG46 nor 52K-8 blocked this binding. These results indicated that the epitopes of NMC-4 and RFF-VⅢRAG : 1 are in close proximity, but those of RG46 and 52K-8 are different, suggesting the epitope heterogeneity of anti-vWF MoAbs which inhibit ristocetin-induced vWF binding.
URI: http://hdl.handle.net/10564/2104
ISSN: 04695550
13450069
Appears in Collections:Vol.40 No.6

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