Post‐Konyne Hepatitis: The Ineffectiveness of Screening for the Hepatitis B Antigen (HBAg)

Sandler, S. Gerald; Rath, Charles E.; Wickerhauser, Milan; Dodd, Roger Y.; Greenwalt, Tibor J.

doi:10.1111/j.1537-2995.1973.tb05478.x

Cited by 32 publications

(8 citation statements)

References 15 publications

(2 reference statements)

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“…Several early studies [9][10][11]22] demonstrated HBsAg reactivity in antihemophilic factor (AHF/factor VIII), Cohn fraction I (fibrinogen), fraction III containing coagulation factors II, VII, IX and X, fractions IV and V containing plas ma protein fraction (PPF), and normal se rum albumin (NSA). The safety of PPF and NSA is ensured by pasteurization at 60 °C for 10 h [10,11] but hepatitis from admin istration of fractions that cannot be heat treated is well documented [7,19,21], in cluding ISG made by zinc precipitation as in Cohn method XII [18], DEAE-chromatography [12], ether fractionation [3], am monium sulfate precipitation [1] or, on oc casion, even Cohn method VI and IX [6,11]. Under these conditions, Cohn fraction II (ISG) rarely contains HBsAg, however, [1^-In a recent report, we described a non denaturing fractionation method for nearly all the clinically useful plasma proteins, us ing solid-phase polyelectrolytes (PEs), which is much simpler and usually gives a higher yield than the Cohn methods for compara tive fractions.…”

mentioning

confidence: 99%

Freedom from Transmission of Hepatitis-B of Gamma-Globulin and Heat-Inactivated Plasma Protein Fraction Prepared from Contaminated Human Plasma by Fractionation with Solid-Phase Polyelectrolytes

Harris¹,

Johnson²,

Semar³

et al. 1979

Vox Sanguinis

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Plasma contaminated with hepatitis B surface antigen (HBsAg) and shown by others to be infectious when injected in a dilution of 1:1,000,000 in chimpanzees, was fractionated by a solid-phase polyelectrolyte (PE) procedure for its content of plasma protein fraction (PPF) and γ-globulin (immune serum globulin; ISG). Quantitative Ausria II radioimmunoassays showed that nearly half the HBsAg was bound by the PE and could be eluted at low pH, while the rest was found in the heat-inactivated PPF. When the ISG was concentrated to 16%, the 13 mg/kg (comparable to a human dose) was injected intramuscularly in 6 chimpanzees, or when the PPF was heated at 60°C for 10 h and injected intravenously in 2 chimpanzees, there was no clinical or laboratory evidence of hepatitis B infection after 12 months, although 1 chimp of 2 who received the same material showed a borderline positive anti-HBsAg antibody result on one of 52 weekly serum samples. Since the new PE fractionation method is essentially nondenaturing, and simpler than the classical ethanol procedures, it was important to establish the noninfectivity of the final products.

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mentioning

confidence: 99%

Freedom from Transmission of Hepatitis-B of Gamma-Globulin and Heat-Inactivated Plasma Protein Fraction Prepared from Contaminated Human Plasma by Fractionation with Solid-Phase Polyelectrolytes

Harris¹,

Johnson²,

Semar³

et al. 1979

Vox Sanguinis

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“…In plasma fractions available for clinical treatment of hemophilia B, factor IX is a minor component. Contamination with activated factor IX and virus particles complicates therapy with thromboembolic disorders and hepatitis (32,33). Affinity chromatography has been widely used for the high yield preparation of plasma proteins (14).…”

Section: Discussionmentioning

confidence: 99%

Immunoaffinity purification of factor IX (Christmas factor) by using conformation-specific antibodies directed against the factor IX-metal complex.

Liebman¹,

Limentani²,

Furie³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

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Factor TX is a vitamin K-dependent blood dotting zymogen that is functionally defective or absent in patients with hemophilia B. A method of imnmunoaffinity chromatogiaphy has been developed for a one-step high yield purification of factor IX directly front plasma. The technique utilizes conformation-specific antibodies that bind solely to the metal-stabilized factor TX conformer, but not to the conformer of factor IX found in the absence of metal ions. Anti-factor IXCa(II) antibodies were immobilized on an agarose matrix. Human plasma in the presence of 7.5 mM MgCI2 was applied to the antibody-agarose column. The factor TX that binds to these antibodies was specifically eluted by metal chelation with EDTA. This immunopurification resulted in a 10,000-fold onestep purification of the fully functional zymogen. Purified factor TX yielded a single band upon gel electrophoresis in NaDodSO4 and had a specific activity of 120-150 units/mg. The purified factor IX was separated from other vitamin K-dependent blood clotting proteins and hepatitis virus; no activated factor TX was detected. This method has application for the large scale purification of factor TX for the treatment of hemophilia B.Factor IX, a vitamin K-dependent plasma protein with a mo- (9), and immunochemical methods using conformation-specific rabbit polyclonal (10) and murine monoclonal antibodies (11) that bind solely to the metal-stabilized conformation.Although we have used these conformation-specific antibodies to develop specific immunoassays for prothrombin species with various contents of y-carboxyglutamic acid (12, 13), we have recently recognized the advantages of conformation-specific antibodies for the immunoaffinity chromatographic purification of proteins. Unlike standard methods for immunopurification, in which the harsh conditions required for the dissociation of the antibody-antigen complex can lead to denaturation and loss of function of the protein (14), this method involves mild and specific elution conditions. Antibodies that only recognize the metal-stabilized conformer of the protein are used to transiently immobilize the protein to a solid support. The antibody-protein complex is disrupted by the removal of bound metal ions from the protein with a metal chelator. The general technique, applied to the purification of factor IX (Christmas factor), has potential application for the large scale purification of factor IX for specific replacement therapy in hemophilia B.

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“…In those days hepatitis was a big problem. The Red Cross Blood Program as the largest collection agency had to be interested in hepatitis 70‐73 . We were selected by Abbot to test their radioimmunoassay procedure for hepatitis B.…”

Section: 9‐ and 10‐week Storage *mentioning

confidence: 99%

Antibodies, antigens, and anticoagulants: a historical review of a lifetime in transfusion medicine—the Landsteiner Lecture 2004

Greenwalt¹

2005

Transfusion

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Post‐Konyne Hepatitis: The Ineffectiveness of Screening for the Hepatitis B Antigen (HBAg)

Cited by 32 publications

References 15 publications

Freedom from Transmission of Hepatitis-B of Gamma-Globulin and Heat-Inactivated Plasma Protein Fraction Prepared from Contaminated Human Plasma by Fractionation with Solid-Phase Polyelectrolytes

Freedom from Transmission of Hepatitis-B of Gamma-Globulin and Heat-Inactivated Plasma Protein Fraction Prepared from Contaminated Human Plasma by Fractionation with Solid-Phase Polyelectrolytes

Immunoaffinity purification of factor IX (Christmas factor) by using conformation-specific antibodies directed against the factor IX-metal complex.

Antibodies, antigens, and anticoagulants: a historical review of a lifetime in transfusion medicine—the Landsteiner Lecture 2004

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