No abstract

Properties of the protein moieties of canine tissue thromboplastins (TTP's) from brain (BTTP), lung (LTTP), arteries (ATTP), AND VEINS (VTTP) were determined. The maximum specific activity of each protein moiety after its relipidation was obtained when the phospholipid-delipidated TTP ratio was 0.32 and was 1,395 U/mg BTTP, 1,130 U/mg LTTP, 630 U/mg VTTP, and 435 U/mg ATTP. The amino acid contents of the protein moieties of LTTP, ATTP, and VTTP were closely similar, but that of BTTP was significantly different. The Ouchterlony analysis showed that BTTP did not react at all with the antibody against VTTP, but that three other TTP's did and showed the reaction of complete identity. Then, the reactivity of 125-I-labeled TTP's with the anti-VTTP antibody was studied. The results showed that 0.79 +/- 0.01 (SD) % of [125I]BTTP, 10.24 +/- 0.5 (SD) % of [125I]LTTP, 19.4 +/- 0.2 (SD) % of [125I]VTTP, and 5.88 +/- 0.4 (SD) % of [125I]ATTP added were bound to the antibody in 2 h. Next, the molecular weight of each was determined by Sephadex G-200 filtration, which averaged 80,000 +/- 4,000 (SD) ([125I]BTTP), 113,000 +/- 5,000 (SD) ([125I]LTTP), 62,000 +/- 3,000 (SD) ([125I]ATTP), and 47,000 +/- 2,000 (SD) ([125I]VTTP). Finally, the plasma behavior of each was studied in four dogs. The plasma half-life averaged 8.1 +/- 0.24 (SD) h ([125I]BTTP), 14.6 +/- 0.5 (SD) h ([125I]LTTP), 7.38 +/- 0.48 (SD) h ([1252]ATTP), and 24.3 +/- 0.9 (SD) h ([125I]VTTP). These results indicate that the protein moieties of canine TTP's from brain, lung, arteries, and veins are closely similar in some aspects but dissimilar in others and are definitely not identical.

No abstract

SummaryProperties of purified and delipidated human tissue thromboplastins (TTPs) from brain (BTTP), lung (LTTP), arteries (ATTP) and placenta (PTTP) were studied. The extinction coefficients were closely similar with a mean value of 8.3 ± 0.01 (SD). The molecular weights were 200,000 ± 3,000 (SD) (BTTP), 90,000 ± 2,000 (SD) (LTTP), 110,000 ± 3,000 (SD) (ATTP) and 250,000 ± 4,000 (SD) (PTTP). The maximum activity of each delipidated TTP after relipidation was obtained when phospholipid-delipidated TTP ratio was 2.0, and the maximum specific activity was 440 units per mg BTTP, 270 units per mg LTTP, 80 units per mg ATTP and 600 units per mg PTTP. Ouchterlony analysis with anti-delipidated PTTP antibody showed the reaction of partial identity between delipidated TTPs and the antibody. Studies of the reactivity of I-125-delipidated TTPs with the antibody gave the following average values for % bound I-125-TTPs in 2 hours: 3.6± 0.2 (SD) % (I-125-BTTP), 11.0± 0.3 (SD) % (I-125-LTTP), 4.4±0.2 (SD) % (I-125-ATTP) and 13.7±0.3 (SD) % (I-125-PTTP). It was also found that the antibody markedly neutralized the coagulant activity of saline extracts of brain, lung and placenta. These results indicate that delipidated BTTP, LTTP, ATTP and PTTP are different while being similar in some aspects and that complete TTPs are not coated with lipids in a manner inaccessible to anti-delipidated PTTP antibody.

The synthesis and catabolism of both prothrombin and PIVKA-II were studied in patients with stable stage of various thromboembolic disorders. Laboratory examinations revealed that their hemostatic and fibrinolytic activities were within normal range. Thirty mg of warfarin was administered orally to patients, which was followed by daily U to 8 mg of warfarin to maintain one stage prothrombin time in therapeutic range. Fifty mg of vitamin K was administered intravenously to these anticoagulated patients. PIVKA-II was determined as prothrombin related antigen in the BaSO^ adsorbed plasma by the method of Ganrot using anti-human prothrombin antibody.After the administration of 30 mg of warfarin, prothrombin clotting activity(FII:C) decreased exponentialy with the half life(T 1/2) of 74 hrs on an average. Rapid increase of PIVKA-II was observed in the early phase of warfarin administration, though in the later phase an increasing tendency slowed down. The changes of PIVKA-II in the early phase could be analyzed easier by following up the changes in the value of (100 - PIVKA-II activity)%. As the progress of time after the administration of warfarin, their values decreased exponentialy with the T 1/2 of 64 hrs on an average. After the administration of vitamin K, FII:C increased rapidly in the initial phase, then slowly returned to normal level. Similarly to the case of PIVKA-II after the administration of warfarin , values of (100 - FII:C activity)% decreased exponentialy with the T 1/2 of 45 hrs on an average. PIVKA-II decreased rapidly after the administration of vitamin K, describing exponential curve with the T 1/2 of 40 hrs on an average.From the results described above, it is suggested that the catabolism of PIVKA-II is much more faster than that of FII:C.