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Biomedical subjects

W H Seegers

Publications and source records attributed to W H Seegers.

At least 19 recordsLinked to original sources
PubMed1986

Postclotting fates of thrombin.

During the clotting of blood, prothrombin is virtually all converted to thrombin. By contrast, Factor X is not. Large quantities of thrombin are inhibited by plasma and platelet AT III (heparin cofactor I), by heparin cofactor II, and by fibrin. Lesser quantities function in various reactions in which thrombin specificity is modified for greater effectiveness. Some thrombin binds to platelets as well as blood vessel endothelial cells, but the latter facts were not included herein.

Animals↗
PubMed1978

Effects of autoprothrombin II-A on epinephrine-induced platelet aggregation of normal- and coumadin-treated dogs.

Platelet-rich plasma from dogs and from coumadin-treated dogs aggregated at the same optimum concentration of epinephrine. Neither protein C nor its active form called autoprothrombin II-A was necessary for aggregation of dog platelets with epinephrine. For platelet aggregation, suboptimal concentrations of epinephrine were potentiated by addition of purified autoprothrombin II-A. The latter, by itself, induced platelet aggregation in high concentration.

Animals↗
PubMed1978

Antithrombin III. Theory and clinical applications. H. P. Smith Memorial Lecture.

Antithrombin III is one of the main inhibitors in the blood coagulation mechanisms. Thrombin and factor Xa are slowly inactivated by it, as well as other serine proteinases of the coagulation mechanisms. Heparin tremendously accelerates the inhibitory function of antithrombin III. In the process antithrombin III activity is also reduced. Heparin retards the thrombin-fibrinogen reaction, but otherwise the effectiveness of heparin as an anticoagulant depends on antithrombin III in laboratory experiments, as well as in therapeutics. The activation of prothrombin is inhibited, and any thrombin or other vulnerable protease that might generate becomes inactivated. The measurement of antithrombin III concentration in blood is now achieved by research methods, as well as by methods that are practical for routine use. The tests require either thrombin or factor Xa as substrate, and could be specific for antithrombin III. There are congenital as well as acquired deficiencies of antithrombin III. The inhibitor is also found in tissues.

Antithrombins↗
PubMed1977

Amino acid sequence of human prothrombin fragments 1 and 2.

The amino acid sequence of the nonthrombin half of human prothrombin is presented. Prothrombin fragment 1 has 155 amino acid residues as compared with 156 for the bovine equivalent. Ten gamma-carboxyglutamic acid residues are at the same location in each species. Human prothrombin fragment 2 contains 118 amino acid residues, as does the similar bovine fragment. Comparing bovine and human prothrombin fragment 1 we found 131 residues to be identical (84%). In prothrombin fragment 2, 84 residues were identical (71%). Assuming a time span of 90 million years since the radiation of several orders of placental mammals, prothrombin fragments 1 and 2 incorporated one substitution site per 100 amino acid sites every 11.2 and 6.3 million years, respectively. Internal homology is acribed to partial gene duplication, with the most likely crossover point located between residues 60-61 and residues 165-166.

Amino Acid Sequence↗
PubMed1977

Autoprothrombin ii-a, thrombin, and epinephrine: interrelated effects on platelet aggregation.

Platelets aggregate with thrombin-free autoprothrombin II-A. Aggregation was dependent on an intact release mechanism since inhibition of aggregation occurred with adenosine, colchicine, or EDTA. Autoprothrombin II-A reduced the sensitivity of platelets to aggregate with thrombin, but enhanced epinephrine-mediated aggregation. Autoprothrombin II-A directly competes for membrane sites sensitive to thrombin. It allows complexes to from with epinephrine. There was no absolute requirement for autoprothrombin II-A since epinephrine aggregated dog platelets at the identical optimum concentration following Coumadin treatment.

Animals↗
PubMed1977

Usefulness of new analytical reagents demonstrated with coumadin-modified plasma.

Prothrombin, factor X or factor IX were removed specifically from bovine plasma by immunological techniques. Each depleted plasma is responsive to the respective purified component, and was used to follow the blood changes produced in a steer's blood by Coumadin administration. A factor IX-VII reagent was also used to follow changes in factor IX and factor VII activity. It is suggested that the new reagents may have practical value for qualitative and quantitative work in blood coagulation studies.

Animals↗