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Nihon Ketsueki Gakkai Zasshi : Journal... Dec 1985
Review
Topics: Amino Acid Sequence; Animals; Antithrombin III; Binding Sites; Blood Coagulation; Heparin; Humans
PubMed: 3915413
DOI: No ID Found -
JAMA Sep 1979
Topics: Antithrombin III; Humans; Methods
PubMed: 480554
DOI: No ID Found -
Seminars in Thrombosis and Hemostasis Oct 1982
Comparative Study Review
Topics: Adolescent; Adult; Antithrombin III; Autoanalysis; Blood Coagulation; Blood Coagulation Tests; Chemical Phenomena; Chemistry; Chromogenic Compounds; Heparin; Humans; Immunodiffusion; Immunoelectrophoresis, Two-Dimensional; Infant, Newborn; Middle Aged; Molecular Weight
PubMed: 6817417
DOI: 10.1055/s-2007-1005059 -
Nihon Rinsho. Japanese Journal of... Mar 1995
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Rinsho Byori. the Japanese Journal of... Apr 1987
Review
Topics: Adult; Antithrombin III; Blood Coagulation Disorders; Female; Humans; Methods
PubMed: 3302389
DOI: No ID Found -
Transfusion May 1998
Review
Topics: Antithrombin III; Antithrombin III Deficiency; Blood Coagulation Disorders; Disseminated Intravascular Coagulation; Female; Humans; Infant, Newborn; Pregnancy; Thrombosis
PubMed: 9633563
DOI: 10.1046/j.1537-2995.1998.38598297219.x -
Hepatology (Baltimore, Md.) Aug 1991Previous studies have shown that antithrombin III levels are low in fulminant hepatic failure, and heparin kinetics are abnormal, making control of heparinization... (Clinical Trial)
Clinical Trial Randomized Controlled Trial
Previous studies have shown that antithrombin III levels are low in fulminant hepatic failure, and heparin kinetics are abnormal, making control of heparinization difficult during hemodialysis of these patients who are at risk of bleeding. In this study, we have performed a controlled, randomized trial of antithrombin III supplementation on heparin activity, occurrence of bleeding and the platelet count and activation during hemodialysis in 24 patients with fulminant hepatic failure. The treated group of 12 patients was given 3,000 units of antithrombin III before hemodialysis. Antithrombin III supplementation was shown to normalize antithrombin III levels during hemodialysis (prelevels: 0.22 +/- 0.03 U/ml S.E.; at 1 hr 0.99 +/- 0.06 U/ml; p less than 0.001; control prelevels: 0.24 +/- 0.03 U/ml; at 1 hr 0.23 +/- 0.04 U/ml). Total heparin usage was significantly decreased by antithrombin III supplementation (median 5,200 U; range = 2,000 to 13,000) as compared with the control group (median 10,200 U; range = 5,000 to 16,500; p less than 0.005). Blood heparin level (antifactor Xa activity) after the initial bolus was significantly greater in the antithrombin III-supplemented subjects (0.40 +/- 0.07 U/ml compared with 0.22 +/- 0.05 U/ml in the control group; p less than 0.05). The significant reduction in platelet count observed in the control patients (18% +/- 6% at 1 hr; p less than 0.05) did not occur in antithrombin III patients (6% +/- 4% at 1 hr), which was reflected by a lower release of the platelet-specific protein beta-thromboglobulin. Two of 12 patients in both groups showed minor bleeding around vascular access sites during the first hemodialysis.(ABSTRACT TRUNCATED AT 250 WORDS)
Topics: Antithrombin III; Blood Platelets; Drug Therapy, Combination; Hemorrhage; Heparin; Humans; Liver Diseases; Platelet Count; Renal Dialysis
PubMed: 1860682
DOI: No ID Found -
Blood Feb 1981Crossed immunoelectrophoretic patterns were obtained on three patients with a congenital deficiency of anti-thrombin III (AT-III), and on normal single donor and...
Crossed immunoelectrophoretic patterns were obtained on three patients with a congenital deficiency of anti-thrombin III (AT-III), and on normal single donor and "pooled" plasma controls. In the presence of heparin (incorporated into the agarose gel matrix), the AT-III of normal human plasma was separated into four components: two major, faster-moving components, and two minor, slower-moving components. The three patients with congenital deficiency of AT-III (levels approximately 50% of normal) appeared to possess only one of the faster-moving components, and one of the slower-moving components.
Topics: Antithrombin III; Antithrombin III Deficiency; Epitopes; Humans; Immunoelectrophoresis, Two-Dimensional; Protein Precursors
PubMed: 6160891
DOI: No ID Found -
The Journal of Biological Chemistry Jan 1985Two distinct forms of antithrombin III were isolated by chromatography of normal human plasma on heparin-Sepharose. The predominant antithrombin species present (AT-III...
Two distinct forms of antithrombin III were isolated by chromatography of normal human plasma on heparin-Sepharose. The predominant antithrombin species present (AT-III alpha), which eluted from the affinity column in 1 M NaCl, was identified as the antithrombin III form which has been previously characterized. Ionic strength of the buffer was increased to elute a variant form of antithrombin III, designated as AT-III beta. The molecular weight of AT-III beta is less than that of AT-III alpha, but physicochemical studies do not indicate measureable differences in the polypeptide portion of the proteins. Carbohydrate determination revealed the sole detectable structural difference in the two antithrombins: levels of hexosamine, neutral sugars, and sialic acid in AT-III beta were all 25-30% less than in AT-III alpha. Kinetic studies of thrombin inactivation by both antithrombins, in the presence of nonsaturating amounts of heparin, indicated that AT-III beta inhibited thrombin more rapidly. AT-III beta is also distinguishable from AT-III alpha on the basis of heparin-binding affinity estimated from titration of protein fluorescence with heparin. Thus, antithrombin III exists as two molecular entities in human plasma which differ both structurally, in carbohydrate content, and functionally, in their heparin-binding behavior.
Topics: Amino Acids; Antithrombin III; Carbohydrates; Enzyme-Linked Immunosorbent Assay; Genetic Variation; Heparin; Humans; Kinetics; Protein Binding
PubMed: 3965464
DOI: No ID Found -
Folia Haematologica (Leipzig, Germany :... 1983In a brief survey, recent data on the molecular structure and functions of antithrombin III as well as on the similarity of identity with antithrombin III of newborns... (Review)
Review
In a brief survey, recent data on the molecular structure and functions of antithrombin III as well as on the similarity of identity with antithrombin III of newborns and mammals are referred to. Moreover, the survival time in circulation and its broad inhibiting spectrum comprising not only all activating factors of coagulation, but also other proteases, is discussed. The accelerating effect of heparin on response and possible mechanisms of this acceleration are discussed. The various procedures of determination are briefly dealt with. Furthermore, the distinct tendency towards thromboembolic complications occurring in patients with only a slight reduction of antithrombin III level is dealt with, as it was described in inherited and acquired deficiency of antithrombin III. Finally, the possibilities of therapy for this deficiency are discussed and is underlined on the key position of antithrombin III for maintaining the balance of coagulation.
Topics: Antithrombin III; Antithrombin III Deficiency; Blood Coagulation; Heparin; Humans; Molecular Weight; Thromboembolism; Time Factors
PubMed: 6194066
DOI: No ID Found