Cross-reacting material in congenital factor VIII deficiencies (Haemophilia A and von Willebrand's disease)

Meyer, Dominique; Lavergne, Jean‐Maurice; Larrieu, M J; Josso, F

doi:10.1016/0049-3848(72)90050-3

Cited by 87 publications

(32 citation statements)

References 9 publications

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“…Our immunological studies largely confirm those reported by others (13)(14)(15)(16)(17)(18). A spontaneously formed human factor VIII inhibitor as well as antiseruim prepared in rabbits to highly purified humani factor VIII clearly neutralized factor VIII activity in specific factor VIII assays.…”

Section: Discussionsupporting

confidence: 80%

“…The studies reported here expand previous observations (1-11) concerning certain properties of nornmal, functional humain factor VIII, and in addition, support immunological data (13)(14)(15)(16)(17)(18) indicating that nonfunctional factor VIII is present in classical hemophilia. Several investigators have shovn that highly purified factor VIII can be prepared by filtering factor VIII concentrates through columns of 2-4% agarose as the final purification step (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11).…”

Section: Discussionsupporting

confidence: 79%

“…While some of the physicochemical properties of humain factor VIII have been determiined( (2)(3)(4)(8)(9)(10)(11), the study of its subunit structure has only been recently approached (5,(10)(11)(12). Particularly in light of the immunological evidence that hemophilic plasma contains nonfunctional factor VIII in quantities comparable to those of functional factor VIII in normal plasnma (13)(14)(15)(16)(17)(18), the characterization of the structures 1 Abbreviationis utscd ini this paper: AHF, antihemophilic factor; MWT, molecular weight; s25s, sedimentation coefficient; SDS, sodium dodecyl sulfate; v, partial specific voluime.…”

Section: Introductionmentioning

confidence: 99%

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The Subunit Structure of Normal and Hemophilic Factor VIII

Shapiro

Andersen²,

Pizzo³

et al. 1973

J. Clin. Invest.

144

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A B S T R A C T Human factor VIII froml nornmals anid hemophiliacs was partially purified by ethaniol and polyethylene glycol precipitations. Final purification was achieved by gel filtration on 2 or 4%Xc agarose or ion1 exchange chromatography on diethylaminoethyl cellulose. Comparable amounts of highly purified protein were obtained from normal and hemophilic plasma following the agarose chromatographv step. Highly purified factor VIII was not dissociated by 6 -MI guanidine hydrochloride or 1% sodium dodecyl sulfate. However, when reduced by P-mercaptoethanol and analyzed by sodium dodecyl sulfate polvacrylamide gel electrophoresis, a single subunit species with an estimiiated 19-5,000 molecular weight was found for both normcal an(d hemiiophilic factor VIII. By sedimiientation equilibrium analysis, the normal factor V-III subunit was homogeneous and had an estimated nmolecular wveight of 202,000. The subunit polypeptides from niormal or hemoplilic factor VIII contained carbohy\drate. Each was homogeneous by isoelectric focusing. Immilllunodiffusion of purified normal and hemoplhilic factor VIII against rabbit aintiserum to purified normiial liuman factor VIII slhowed a single line of precipitationi. V-erv low concenitr-ations of purified humiian thrombin initially increased the activitv of normal factor VIII about threefold and tlhen progressively destroyed activity by 3 h. Only-minimal activation occurred with hemiiophilic factor VIII. Both the activation and inactivation of normal alnd hemo-

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Section: Discussionsupporting

confidence: 80%

Section: Discussionsupporting

confidence: 79%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

The Subunit Structure of Normal and Hemophilic Factor VIII

Shapiro

Andersen²,

Pizzo³

et al. 1973

J. Clin. Invest.

144

View full text Add to dashboard Cite

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“…The assay described herein may therefore provide a method for quantitatively measuring the amount of "anti-bleeding factor" in plasma and be useful for studying patients with bleeding disorders. Since patients with von Willebrand's disease are also deficient in both the antihemophilic factor procoagulant activity (VIIIAHF) and factor VIII antigen (VIIIAGN) (7,(18)(19)(20), the presence of the von Willebrand factor on the same molecule as these other two activities should be considered. Recent studies indicate that factor VIII is a glycoprotein whose molecular weight as determined in vitro is in excess of 2 X 108 (21)(22)(23)(24).…”

Section: Assay Of the Von Willebrand Factor (Viiivwf )mentioning

confidence: 99%

Quantitative Assay of a Plasma Factor Deficient in von Willebrand's Disease that is Necessary for Platelet Aggregation. RELATIONSHIP TO FACTOR VIII PROCOAGULANT ACTIVITY AND ANTIGEN CONTENT

Weiss¹,

Hoyer²,

Rickles³

et al. 1973

J. Clin. Invest.

424

168

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A B S T R A C T In a previous paper, we showed that the abnormality of ristocetin-induced platelet aggregation in platelet-rich plasma in 10 patients with von Willebrand's disease could be corrected by a factor in normal plasma that was present in the same fractions as factor VIII procoagulant activity (antihemophilic factor, AHF, VIIIAHF) when prepared by chromatography on BioGel 5 M (Bio-Rad Laboratories, Richmond, Calif.). This observation suggests that patients with this disorder are deficient in a plasma factor, associated with the factor VIII molecule, that is necessary for normal platelet function. In the present paper, we describe, an assay for this factor, the von Willebrand factor (VIIIvwF), based on the observation that a log-log relationship exists between the amount of ristocetin-induced aggregation of washed, normal platelets and the concentration of normal plasma present in the test system. We assayed the activity of VIIIvwF as well as antihemophilic factor procoagulant activity (VIIIAHF) and factor VIII antigen (VIIIAGN)

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“…Recent studies, employing an antiserum raised in rabbits to highly purified preparations of normal human AHF, have indicated that the plasma of hemophilic subjects contains normal or increased quantities of an antigen precipitating with this antiserum, whereas that of patients with von Willebrand's disease has quantities of this antigen reduced in proportion to the reduction of AHF clot-promoting activity (1)(2)(3)(4)(5). The antisera used in our earlier studies had the following characteristics: on immunodiffusion they produced a line of identity between hemophilic and normal plasma or purified AHF prepared from normal plasma; on immunoelectrophoresis they produced single precipitin lines of similar mobility with concentrates of normal or hemophilic plasma, and they inhibited the clot-promoting activity of normal plasma in specific assays of AHF activity.…”

Section: Introductionmentioning

confidence: 99%