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01121 Journal of Nara Medical Association >
Vol.40 No.6 >

Please use this identifier to cite or link to this item: http://hdl.handle.net/10564/2102

Title: von Willebrand因子(vWF)フラグメント(97 kDa,52/48 kDa,及びFⅢ-T2) と抗vWFモノクローナル抗体NMC-4の免疫反応性
Other Titles: IMMUNOREACTIVITY OF AN ANTI-VON WILLEBRAND FACTOR (VWF) MONOCLONAL ANTIBODY NMC-4 WITH SOME TRYPTIC VWF FRAGMENTS (97 kDa, 52/48 kDa, FⅢ-T2 FRAGMENTS)
Authors: 新家, 興
武田, 以知郎
中井, 寛明
西尾, 健治
宮田, 茂樹
嶋, 緑倫
吉岡, 章
福井, 弘
藤村, 吉博
Keywords: vWF fragments
Western blotting
ristocetin
botrocetin
NMC-4
Issue Date: 31-Dec-1989
Publisher: 奈良医学会
Citation: 奈良医学雑誌 Vol.40 No.6 p.791-796
Abstract: We have shown that an anti-von Willebrand factor (vWF) monoclonal antibody designated as NMC-4 blocks both the ristocetin- and botrocetin-induced (¹²⁵Ⅰ) vWF bindings to platelet glycoprotein (GP)Ⅰb. Using NMC-4 coupled Sepharose 4B column or electroelution apparatus, a 97 kDa fragment and a 130 kDa fragment were distinctively purified from a whole tryptic digest of vWF. The 97 kDa fragment, which was shown to be a homodimer of the amino acid residue 449-728 of vWF subunit, retained the activity to inhibit both the ristocetin- and botrocetin-induced (¹²⁵Ⅰ) vWF binding to GPⅠb as found in the parent molecule. Another vWF fragment, the FⅢ-T2 fragment, which is a twin heterodimer composed of two H-chains (residue 273-511) and two L-chains (residue 674-728) held together by disulfide-bonds, was also purified by high pressure liquid chromatography. FⅢ-T2 fragment showed no inhibitory effect on botrocetin-induced vWF binding to GPⅠb, whereas it blocked the ristocetin-induced vWF binding. On Western blotting analysis and dot blot assay, NMC-4 failed to react with both the reduced and nonreduced FⅢ-T2 fragment. These results indicate that the vWF binding domains to GPⅠb expressed by either ristocetin or botrocetin are different and the amino acid residue Leu512-Lys673 is important for both botrocetin-induced vWF binding and NMC-4 binding.
URI: http://hdl.handle.net/10564/2102
ISSN: 04695550
13450069
Appears in Collections:Vol.40 No.6

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