A new ion-exchange chromatographic procedure has been developed to produce a highly purified factor VIII (FVIII) concentrate from plasma cryoprecipitate. Solubilized cryoprecipitate, after adsorption on aluminium hydroxide and cold precipitation, was treated with 0.3% tri(n-butyl)phosphate and 1% Tween 80 at 25 degrees C for at least 8 h to inactivate lipid-enveloped viruses. The fraction was then loaded onto a column packed with DEAE-Fractogel TSK 650 M and chromatographed. Most proteins and TnBP-Tween 80 flowed through the gel unretarded. FVIII:c, which bound to the gel, was eluted by increasing the ionic strength, then was directly filter-sterilized without ultrafiltration or addition of a protein stabilizer. Chromatographic recovery of FVIII:c was 80-90%. After freeze-drying, FVIII:c was at a concentration of 42.5 +/- 9.5 IU/ml and had a specific activity of 175.4 +/- 37.8 IU/mg (n = 40), corresponding to a purification factor of over 12,000 from plasma. The typical yield of the freeze-dried FVIII:c from cryoprecipitate was 55-65%. FVIII:c was stable for over 24 h at room temperature in the liquid state. The mean content of fibrinogen and immunoglobulin G was only 65 and 100 mg/l, respectively, corresponding to 1.4 and 2.3 mg/1,000 IU FVIII:c. This concentrate, which is much purer than traditional FVIII concentrates, has been found to be well tolerated and effective in clinical treatment of hemophilia A patients.

A highly purified factor VIII:c concentrate prepared from cryoprecipitate by ion-exchange chromatography.

An adverse pulmonary reaction to cryoprecipitate in a hemophiliac.

This review is intended to be a critical state-of-the-art overview of the activation and inhibition of the proteins (factor XII, prekallikrein, high molecular weight kininogen, and factor XI) of the contact phase of coagulation. Specifically, this review will reconsider the concept of the reciprocal activation of the proteases of the contact phase of coagulation, factor XII, and prekallikrein, in light of much recent evidence indicating that factor XII, itself, autoactivates when associated with negatively charged surfaces. In addition, the mechanisms for amplification of activation of the proteins of the contact phase of coagulation will be discussed from the pivotal role of high molecular weight kininogen, or one of its altered forms, serving as a cofactor to order the activation of the zymogens it is associated with. The role and relative importance of each of the naturally occurring plasma protease inhibitors (C1-inhibitor, alpha-2-macroglobulin, alpha-1-antitrypsin, antithrombin III, and alpha-1-antiplasmin) will be assessed as they relate to the dampening of contact phase activation. Finally, the contact phase of coagulation activation will be discussed not only as a plasma proteolytic mechanism, but also as it interacts with platelets.

The contact activation system: Biochemistry and interactions of these surface-mediated defense reactions

https://www.amjmed.com/article/0002-9343(66)90006-4/pdf

Major surgery in classic hemophilia using fraction I: Experience in twelve operations and review of the literature

The partial thromboplastin time test provides a convenient and sensitive screening procedure for deficiencies of thromboplastic factors, especially factors VIII and IX. The test is carried out after preincubating the plasma for 10 minutes with kaolin, and Inosithin is used as a platelet substitute. The ;normal range' of the test has been estimated in terms of the differences encountered between random normal plasmas tested in pairs, because individual patients are usually tested against single control subjects. A patient's partial thromboplastin time should be regarded as abnormal if it is more than six seconds longer than the control time. In the diagnosis of haemophilia, patients' plasmas with concentrations of factor VIII as low as about 20% might be regarded as being within the range of normal, if the selected control subject's factor VIII happened to lie near the lower end of the normal range. When mild haemophilia is suspected, discrimination may be improved by diluting both the patient's and the control plasmas 1 in 20 in haemophilic plasma. With the test modified in this way the clotting time is prolonged, though the range of differences among normal subjects is unaltered, and plasmas with factor VIII concentrations below about 30%, i.e., in undiluted plasma, would be unlikely to be regarded as normal. The partial thromboplastin time may be similarly modified as a screening test for factor IX deficiency.Some clinical examples are reported.

https://jcp.bmj.com/content/jclinpath/18/4/465.full.pdf

Partial thromboplastin time test with kaolin: Normal range and modifications for the diagnosis of haemophilia and Christmas disease

SINCE Kekwick and Wolf (1957) described the separation of a globulin fraction of human plasma rich in antihaemophdic factor and its use in six haemophilic patients, it has been possible to prepare this fraction on a limited scale and use it to control spontaneous and traumatic haemorrhage or haemorrhage occurring during surgical operations in patients suffering from classical haemophdia at Lewisham Hospital, Hammersmith Hospital and the Radcliffe Infirmary and Churchill Hospital between 1956 and 1960. The fraction has also been used on a few occasions at other hospitals. This paper describes the plasma fractions used, brief details of the patients, their response to treatment and the transfusion reactions observed in some patients and reports the conclusions derived from this more extensive clinical experience. The concentration of antihaemophilic factor is expressed in one or other of two ways: (i) as a percentage of the normal plasma concentration taken as IOO per cent, (ii) as units, described by Wolf (1956), the average normal plasma concentration being 13.2 units per ml. (range 8-18 units per ml.). The abbreviation AHF is used to denote antihaemophilic factor. The term human antihaemophdic globulin concentrate (AHG concentrate or HAHG) is used to denote the globulin fraction of human plasma rich in antihaemophilic factor. The clinical severity of the disease was graded according to the criteria described by Biggs and Macfarlane (1958).

Further Experience with a Concentrate Containing Human Antihaemophilic Factor

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Further Experience with a Concentrate Containing Human Antihaemophilic Factor