Immunological Differentiation of Three Types of Hæmophilia and Identification of Some Female Carriers

Bennett, Enid; Huehns, E. R.

doi:10.1016/s0140-6736(70)92129-x

Cited by 84 publications

(26 citation statements)

References 10 publications

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“…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: 91%

“…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: 91%

Section: Introductionmentioning

confidence: 99%

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

show abstract

“…In contrast, the plasma of patients with von Willebrand's disease was deficient both in AHF clotpromoting activity and this antigen (1,2). These results have been confirmed by a number of studies (3)(4)(5)(6).…”

Section: Introductionsupporting

confidence: 72%

Studies on the Response of Patients with Classic Hemophilia to Transfusion with Concentrates of Antihemophilic Factor

Bennett¹,

Ratnoff²

1972

J. Clin. Invest.

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“…DISCUSSION Zimmerman, Ratnoff, and Powell (6) using quantitative i,mmunoelectrophoresis, showed that patients with von Willebrand's disease had reduced levels of AHF-like antigen, while plasma of patients with classic hemophilia contained normal quantities of AHF-like antigen. Earlier studies, which employed a variety of antibody preparations, had produced less clear-cut results (9-11), but several groups have now confirmed this finding (12)(13)(14)(15).…”

Section: Methodsmentioning

confidence: 99%

Immunologic Studies in von Willebrand's Disease

Bennett¹,

Ratnoff²,

Levin³

1972

J. Clin. Invest.

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A B S T R A C T Antihemophilic globulin (AHF, factor VIII) levels were measured by a standard coagulation assay and by an immunological technique before and serially after infusion of fresh frozen plasma or cryoprecipitate into patients with von Willebrand's disease. Initial levels of AHF, measured both as procoagulant and as antigen, were low. Immediately after transfusions, the rise in levels of AHF-like antigen was compatible with the quantity of antigen present in the infused plasma or cryoprecipitate. Thereafter, levels of antigen declined rapidly and reached preinfusion values in approximately 24 hr. In contrast, procoagulant activity remained elevated, and sometimes continued to rise, for longer periods of time. One possible explanation of this finding is that the AHF molecule produced by patients with von Willebrand's disease, in response to transfusion of as yet unidentified factors, lacks the antigenic site associated with the normal AHF molecule or the inactive molecule produced by patients with hemophilia A.

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Immunological Differentiation of Three Types of Hæmophilia and Identification of Some Female Carriers

Cited by 84 publications

References 10 publications

The Subunit Structure of Normal and Hemophilic Factor VIII

The Subunit Structure of Normal and Hemophilic Factor VIII

Studies on the Response of Patients with Classic Hemophilia to Transfusion with Concentrates of Antihemophilic Factor

Immunologic Studies in von Willebrand's Disease

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