Thromb Haemost 1982; 47(01): 056-058
DOI: 10.1055/s-0038-1657125
Original Article
Schattauer GmbH Stuttgart

Biochemical and Functional Study of Antithrombin III in Newborn Infants

M M McDonald
The Departments of Medicine and Pediatrics, University of Colorado School of Medicine, Denver, Colorado, U.S.A.
,
W E Hathaway
The Departments of Medicine and Pediatrics, University of Colorado School of Medicine, Denver, Colorado, U.S.A.
,
E B Reeve
The Departments of Medicine and Pediatrics, University of Colorado School of Medicine, Denver, Colorado, U.S.A.
,
B D Leonard
The Departments of Medicine and Pediatrics, University of Colorado School of Medicine, Denver, Colorado, U.S.A.
› Author Affiliations
Further Information

Publication History

Received 11 November 1981

Accepted 28 December 1981

Publication Date:
13 July 2018 (online)

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Summary

Antithrombin III (AT-III) was isolated by heparin affinity chromatography from adult venous and newborn term and preterm umbilical cord blood. The purified proteins were compared by SDS-PAGE, rocket immuno-electrophoresis, protein concentration by microbiuret relative to optical density at 280 nm, heparin cofactor specific activity, progressive neutralization of thrombin and factor Xa at 37°C and pH related antithrombin kinetics. The structural evaluations revealed a fetal AT-III of molecular weight, charge and electrophoretic migration indistinguishable from adult AT-III. The functional studies showed that, on an equimolar basis, the rates of thrombin and Xa interactions with fetal AT-III were as rapid as those with adult AT-III. The catalytic rates of various concentrations of heparin were also equal. The newborn infant, therefore, displays a quantitative but not qualitative deficiency of AT-III.