Stability of VIII:C in plasma: The dependence on protease activity and calcium

Rock, G.; Cruickshank, W.H.; Tackaberry, Eilleen S.; Ganz, Peter; Palmer, Douglas S.

doi:10.1016/0049-3848(83)90347-x

Cited by 54 publications

(35 citation statements)

References 18 publications

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“…Factor VIII .tea p s The one-stage procoagulant assay for VIILC was carried out according to the procedure of Breckenridge and Ratnoff [9] as modified by Rock et al [10]. Thromboscreen reference plasma (Pacific Hemosta sis, Bakersfield, Calif.) was used as the VIILC stan dard.…”

Section: Dda Vp Assaymentioning

confidence: 99%

Intravascular Coagulation Phenomena Associated with Prevalent Fall in Fibrinogen and Plasminogen during <i>L</i>-Asparaginase Treatment in Leukemic Children

Legnani¹,

Palareti²,

Pession

et al. 1988

Pathophysiol Haemos Thromb

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12 children affected by acute lymphoblastic leukemia had higher baseline levels of Normotest, Antithrombin III activity (AT III:A) and antigen (AT IIl·Ag) than those found in the control group, due to increased liver protein synthesis, as shown by the higher values of 30511bumin. Treatment with L-asparaginase (L-Asp) induced a marked decrease in fibrinogen and plasminogen and only a slight but significant reduction in AT III:A, AT III:Ag, protein C and α₂ antiplasmin levels. Platelet counts progressively increased. Each single L-Asp administration acutely induced (as recorded in the 2-hour postadministration samples) a significant increase in fibrinopeptide A values and reduction in several factors and inhibitors, due to activation of coagulation and consumption phenomena. It is suggested that these acute changes, but not the marked and selective reduction in fibrinogen and plasminogen, were partly compensated during L-Asp treatment by an overall increase in clotting and nonclotting protein synthesis in the liver.

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Section: Dda Vp Assaymentioning

confidence: 99%

Intravascular Coagulation Phenomena Associated with Prevalent Fall in Fibrinogen and Plasminogen during <i>L</i>-Asparaginase Treatment in Leukemic Children

Legnani¹,

Palareti²,

Pession

et al. 1988

Pathophysiol Haemos Thromb

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“…A modification of the liquid-phase immunoradiometric assay originally described by Lazarchick and Hoyer [26] was used to measure the factor VIII antigen (F.VIII:Ag) [27]. F.VIII : Ag was also measured using monoclonal antibodies in an ELISA method [28].…”

Section: Collection and Separation Of Bloodmentioning

confidence: 99%

“…Ten bags of heparinized plasma (approximately 250 ml each) were thawed at 4°C for 2 h to prepare cryoprecipitate. After centrifugation [24], the pellets were resolubilized at 37 "C with buffer A [25 mM sodium acetate, 0.9% w/v NaCl, 8 units/ml heparin, 0.8 pM phenylalanyl-prolyl-arginine chloromethane (Phe-Pro-ArgCH2C1) pH 6.51. The resolubilized cryoprecipitates were then pooled and fractionated further by addition of poly(ethyleneglyco1) (4000) to 4.0% (w/v) and to 11 % (w/v) essentially as described previously [22].…”

Section: Preparation Effactor Vzzimentioning

confidence: 99%

“…For example, we have shown that collection of blood into heparin, rather than into chelating anticoagulants such as EDTA or citrate, increases the recovery of factor VIII several-fold [21 -231. This is due, in part, to heparin's ability to maintain physiological calcium levels [24]. The beneficial effects of heparin may be further amplified by its ability to inhibit various plasma proteases which are known to inactivate factor VllI [24].…”

mentioning

confidence: 99%

“…This is due, in part, to heparin's ability to maintain physiological calcium levels [24]. The beneficial effects of heparin may be further amplified by its ability to inhibit various plasma proteases which are known to inactivate factor VllI [24].…”

mentioning

confidence: 99%

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Human factor VIII from heparinized plasma

Ganz

Tackaberry

Palmer

et al. 1988

European Journal of Biochemistry

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Human factor VIII was purified from heparinized blood by cryoprecipitation, poly(ethyleneglyco1) precipitation, Affi-Gel blue, aminohexyl, polyelectrolyte E5 and immunoaffinity chromatography. A purification of 280000-fold over plasma with a specific activity over 5300 units/mg was achieved. Analyses of factor VlII using HPLC indicated a molecular mass of 280-340 kDa. Variation in the native mass may reflect heterogeneity of the protein due to associated lipid since structural analysis confirmed that factor VIII contained variable amounts of free fatty acids and diglycerides and triglycerides, but no phospholipids. Additional characterization by denaturing polyacrylamide gel electrophoresis under reducing conditions, followed by silver staining, showed a major single-chain polypeptide of factor VIII with a mass of approximately 260 kDa. To determine whether proteolyzed forms of factor VIII were present during fractionation, we analysed earlier steps in purification. This revealed additional species of factor VIII eluting faster than the single-chain form during chromatography on polyelectrolyte E5. Gel electrophoresis showed that these species of factor VIII consisted of multiple polypeptide chains, and partial peptide mapping using Staphylococcus aureus V8 protease indicated that they were structurally related. Monoclonal and hemophilic antibodies were used in immunoadsorption experiments to demonstrate that the purified factor VIII was composed predominantly of the 260-kDa factor VIII chain.Blood coagulation depends upon the sequential activation of a large number of plasma proteins, culminating in the formation of an insoluble net of fibrin which serves to stabilize a platelet plug at the site of blood vessel injury.One of the key steps in the coagulation process is the activation of factor X to X,. In the intrinsic pathway this reaction is catalyzed by factor IX, in concert with factor VIII, calcium ions and phospholipids [I -51. A number of lines of evidence support the view that factor VIII participates as a regulatory protein or cofactor in the activation of factor X [6, 71, and that proteolytic activation of factor VIII by factor X,, factor IX, or thrombin may be a necessary prerequisite for full expression of procoagulant activity [4, 8 -

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Fractionation, Blood, Plasma Fractionation

Foster

2000

Kirk-Othmer Encyclopedia of Chemical Technology

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Blood plasma fractionation is a biopharmaceutical manufacturing operation in which high quality, proteinaceous products are prepared for clinical use from human plasma. Products prepared in this manner include albumin, eg, human serum albumin, and plasma protein fraction, for volume and protein replacement in surgery and for the treatment of injury and disease; coagulation factors, eg, Factor VIII and Factor IX Complex, for the prevention and treatment of bleeding disorders; and immunoglobulins, eg, immune serum globulin and immune globulin intravenous, for the prevention and treatment of infectious diseases and immune disorders. A number of highly integrated bioseparation processes are employed to fractionate human plasma into its different constituents. These range from established cold‐ethanol precipitation technology, devised in the 1940s, to more recently developed solid‐phase adsorption/desorption techniques. The principal developments since 1980 have been immunoglobulin products for intravenous use, and highly effective technologies for the inactivation of viral contaminants, such as hepatitis viruses and Human Immunodeficiency Virus (HIV), which were associated with earlier coagulation factor preparations.

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Stability of VIII:C in plasma: The dependence on protease activity and calcium

Cited by 54 publications

References 18 publications

Intravascular Coagulation Phenomena Associated with Prevalent Fall in Fibrinogen and Plasminogen during <i>L</i>-Asparaginase Treatment in Leukemic Children

Intravascular Coagulation Phenomena Associated with Prevalent Fall in Fibrinogen and Plasminogen during <i>L</i>-Asparaginase Treatment in Leukemic Children

Human factor VIII from heparinized plasma

Fractionation, Blood, Plasma Fractionation

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