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1.

001-es BibID:BIBFORM034913
Első szerző:Tornai István (belgyógyász, gasztroenterológus)
Cím:Von Willebrand faktor-ellenes monoklonális antitestek kísérletes és gyakorlati alkalmazása / Tornai István, Arnout Jef, Deckmyn Hans, Declerck Paul, Peerlinck Kathelijne, Boda Zoltán, Vermylen Jos
Dátum:1994
Tárgyszavak:Orvostudományok Klinikai orvostudományok magyar nyelvű folyóiratközlemény hazai lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:Magyar Belorvosi Archívum. - 47 : 6 (1994), p. 441-447. -
További szerzők:Arnout, Jef Deckmyn, Hans Declerck, Paul J. Peerlinck, Kathelijne Boda Zoltán (1947-) (belgyógyász, haematologus, klinikai onkológus) Vermylen, Jozef
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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2.

001-es BibID:BIBFORM034911
Első szerző:Tornai István (belgyógyász, gasztroenterológus)
Cím:Measurement of von Willebrand Factor Antigen in Plasma and Platelets with an Enzyme-Linked Immunosorbent Assay Based on Two Murine Monoclonal Antibodies / I. Tornai, P. J. Declerck, L. Smets, J. Arnout, H. Deckmyn, K. M. J. Caekebeke-Peerlinck, J. Vermylen
Dátum:1991
ISSN:0301-0147
Megjegyzések:Two murine monoclonal antibodies, raised against von Willebrand factor (vWF), were used to construct an enzyme-linked immunosorbent assay (ELISA), for quantitation of vWF antigen (vWFAg) in human plasma and platelets. This assay had a lower limit of sensitivity of 0.0001 IU/ml in buffer, and thus is one to two orders of magnitude more sensitive than other ELISA assays which have been reported. The intraassay, interassay and interdilution coefficients of variation were 4.1, 10.4 and 9.9%, respectively. In normal plasma (n = 20), the vWFAg level was 0.83 (range: 0.42-1.25) IU/ml. In normal washed platelets (n = 10), 0.35 (0.25-0.49) IU/10(9) platelets was found. In plasma obtained from various patient groups the following vWFAg levels (geometric mean and range) were observed: von Willebrand's disease (n = 19): 0.18 (0.02-0.77) IU/ml; patients with liver cirrhosis (n = 20): 3.73 (1.68-9.20) IU/ml; patients with pregnancy-induced hypertension (n = 20): 4.14 (2.28-7.44) IU/ml and patients with malignant disease (n = 10), 2.54 (1.51-5.60) IU/ml. A linear correlation was found between vWFAg levels measured with a polyclonal antibody based Laurell electroimmunoassay (r = 0.92, n = 58) or with a polyclonal antibody based ELISA (r = 0.94, n = 64). The present assay is based on stable and reproducible reagents and allows the specific measurement of vWFAg in plasma and in platelets. This assay may constitute a useful tool for the further investigation of clinical conditions associated with changes in vWFAg levels. In addition, its high sensitivity may facilitate a more detailed study of platelet vWFAg in normal and in pathological conditions.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Monoclonal antibodies
külföldön készült közlemény
Immunosorbent assay
Plasma von Willebrand factor
Platelet von Willebrand factor
Megjelenés:Hemostasis. - 21 : 3 (1991), p. 125-134. -
További szerzők:Declerck, Paul J. Smets, L. Arnout, Jef Deckmyn, Hans Caekebeke-Peerlinck, K. M. J. Vermylen, Jozef
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
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3.

001-es BibID:BIBFORM034425
035-os BibID:(PMID)8423224
Első szerző:Tornai István (belgyógyász, gasztroenterológus)
Cím:A monoclonal antibody recognizes a von Willebrand factor domain within the amino-terminal portion of the subunit that modulates the function of the glycoprotein IB- and IIB/IIIA-binding domains / Istvan Tornai, Jef Arnout, Hans Deckmyn, Kathelijne Peerlinck, Jos Vermylen
Dátum:1993
ISSN:0021-9738 1558-8238
Megjegyzések:We developed a monoclonal antibody, 1C1E7, against vWf that increases ristocetin-induced platelet aggregation in a dose-dependent manner and lowers the threshold concentration of ristocetin needed to obtain a full aggregatory response. The platelet aggregatory effect of asialo vWf (ASvWf) also is enhanced by 1C1E7, in the presence or absence of glycoprotein (GP) IIb/IIIa receptor antagonism. In the presence of ristocetin, both intact 1C1E7 and its Fab fragments enhance specific binding of 125I-vWf to platelets. With 1C1E7, the intermediate and higher molecular weight multimers of vWf are preferentially bound to both GP Ib and GP IIb/IIIa. Thrombin-induced 125I-vWf binding to GP IIb/IIIa also is increased by 1C1E7. Maximal binding of 1C1E7 to vWf corresponds to 0.97 mol/mol vWf monomer with a Kd of 4.7 x 10(-10) M. 1C1E7 reacts with a 34/36-kD tryptic fragment (III-T4) and a 34-kD plasmic fragment (P34), which localizes the epitope between amino acid residues 1 and 272; this was confirmed by NH2-terminal amino acid sequencing. Finally, platelet aggregation by ASvWf was associated with a sharp rise in intracellular Ca2+ only in the presence of 1C1E7. An antibody-mediated conformational change of vWf may result in an improved presentation of the GP Ib- and GP IIb/IIIa-binding domains of mainly the larger multimers; the increased density of vWf on the platelet surface leads to platelet activation. The antibody may thus recognize a domain of relevance for vWf physiology.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
külföldön készült közlemény
Megjelenés:The Journal of Clinical Investigation. - 91 : 1 (1993), p. 273-282. -
További szerzők:Arnout, Jef Deckmyn, Hans Peerlinck, Kathelijne Vermylen, Jozef
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
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