Contributions to the Optimal Use of Human Blood

Ef, Vogelaar; Berg, Boer-v d; Hg, Brummelhuis; Sp, Beentjes; Hw, Krijnen

doi:10.1111/j.1423-0410.1974.tb02409.x

Cited by 7 publications

(4 citation statements)

References 11 publications

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“…The antibody titers of S-GG are almost equal to those of the original GG in the case of antibodies against toxins and viruses, which are likely to belong to the IgG class [15], Some BA activities were considerably decreased which would probably be due to the splitting of IgM pentamers into mono mers [12], The biological half-life of Ssulfonated antibody was found to be as long as that of intact antibody, while the half…”

Section: Discussionmentioning

confidence: 91%

Development of an Intravenous γ-Globulin with Fc Activities

Masuho¹,

Tomibe²,

Matsuzawa³

et al. 1977

Vox Sanguinis

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S-sulfonated γ-globulin (S-GG) was prepared by treating γ-globulin with sulfite and tetrathionate ions. About four interchain disulfide bonds were selectively cleaved to give S-sulfonate groups. Although the above treatment strongly suppresses anticomplementary activity and nonspecific skin reactivity, the resulting S-GG retains high antibody activity. Furthermore, S-GG was found to maintain satisfactory levels for prolonged periods in vivo. The physicochemical and antigenic analyses of S-GG suggest that the S-sulfonation induces structural modification only at restricted sites.

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Section: Discussionmentioning

confidence: 91%

Development of an Intravenous γ-Globulin with Fc Activities

Masuho¹,

Tomibe²,

Matsuzawa³

et al. 1977

Vox Sanguinis

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“…The paste obtained when fractionating [6] plasma pools of 150-400 I with an anti-D content of ±10 /<g/ml was frozen and stored for 1-4 years at -30°C before processing.…”

Section: Methodsmentioning

confidence: 99%

“…The distribution of various immunoglobulins and antibody activities in the fractions of human plasma as obtained by a modified Cohn VI plasma fractionation system has been described earlier [6].…”

Section: Introductionmentioning

confidence: 99%

“…The method was developed on the basis of results obtained with experiments on a small scale in which the influences of different pH, ionic strength, protein and ethanol concentrations on suspensions of fraction III were studied. It was noticed that the pH influenced the solubility of anti-D activity during the separation of fraction III and its supernatant [6]. Under conditions of (almost) constant ionic strength, fixed protein and ethanol concentrations and temperature the solubility of anti-D activity was optimal at pH 4.5.…”

Section: Introductionmentioning

confidence: 99%

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Contributions to the Optimal Use of Human Blood

Vogelaar¹,

Berg²,

Reijnierse³

et al. 1974

Vox Sanguinis

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It was observed that during the preparation of normal anti-D immunoglobulin concentrates by a modified Cohn VI method a considerable loss of anti-D activity occurred in fraction III. A method was developed to prepare anti-D immunoglobulin concentrates from fraction III by ethanol fractionation. Three batches were treated on a production scale. An average of 18% of the amount of anti-D activity present in the original plasma, was recovered, which increased the total yield of anti-D activity from 44 to 62%. The specific activity of anti-D in the concentrate thus prepared was 2-3 times higher than that in the normal anti-D immunoglobulin concentrate. The anti-D immunoglobulin concentrate prepared from fraction III was diluted with normal immunoglobulin concentrate to reach an anti-D concentration of 110-120 µg/ml. Using several analytical procedures no essential differences could be demonstrated between this final product and the normal immunoglobulin concentrate. After 8 months of storage at 4°C no significant decrease in anti-D activity could be demonstrated.

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Ethanol Fractionation of Human Plasma: An Overview

Brummelhuis¹

1985

Plasma Fractionation and Blood Transfusion

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Human plasma is an extraordinarily complex aqueous solution of proteins, hormones, lipoids, carbohydrates etc., from which certain proteins are of interest in therapy. At the moment a small but increasing number of the hundreds of plasma proteins are used in clinical medicine and have to be prepared by fractionation. The methods applied in fractionation are more or less the same as for purification of proteins, but the aim is quite different; fractionation is meant to make the most out of plasma in terms of the clinical efficacy of the wanted protein(s). The safety of the preparations must be guaranteed by avoiding possible changes ill the native structure of the protein(s) or contamination that causes side effects. The economics of fractionation also have to be considered. To reach this aim, good recovery and efficacy of the protein(s) are necessary and are mainly dependent on controlled methods and technology. The safety is dependent mainly on a correct interpretation of "Good Manufacturing Practices", which primarily is to be found in well instructed and well educated personnel, adequate housing, sanitation and equipment. Continuous attention is needed to control the costs.During the last forty years a number of methods have been tried and performed in the fractionation of human plasma based on: differential solubility differential interaction with solid media differential interaction with physical fields. For the preparation of the bulk plasma proteins, i.e. fibrinogen, immunoglobulin and albumin, the cold ethanol method, based on different solubility is generally practised although other methods based on different solubility are or have been used like fractionation with ammonium sulphate (1) and ether(2).The separation between the proteins is performed under conditions where either the solubility of the desired protein is maximized and the solubility of the other proteins is minimized or reversed. The precipitate is separated from the supernatant by semi-continuous centrifugation and if needed, clarification.Variables determining the precipitation of the protein(s) are: ethanol concentration pH temperature ionic strength protein concentration from which the last two are less critical than the other variables and therefore mostly left out of the fractionation schemes. The first large scale batch wise fractionation of human plasma using acetate buffers was described by Cohn and coworkers who developed a number of methods from which the method 5 and 6 (3) and the immunoglobulin method 9 according to Oncley et aI. (4) are the best known.In the flowsheet ( fig. 1) other products like plasminogen, prothrombin complex etc., which can be prepared from fraction II+III and a further purification of fraction II has been left out. By this combined method five preparations can be derived from human plasma: C. T. Smit Sibinga et al. (eds.), Plasma Fractionation and Blood Transfusion

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Contributions to the Optimal Use of Human Blood

Cited by 7 publications

References 11 publications

Development of an Intravenous γ-Globulin with Fc Activities

Development of an Intravenous γ-Globulin with Fc Activities

Contributions to the Optimal Use of Human Blood

Ethanol Fractionation of Human Plasma: An Overview

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