THE PREPARATION OF SUCROSE-C14 WITH HIGH SPECIFIC ACTIVITY AND HIGH TRACER YIELD USING DETACHED SUGAR BEET LEAVES

Radioactive sucrose, in millicurie amounts, was prepared by feeding a detached sugar beet leaf C14O2 in air for 15 to 20 minutes followed by 5 to 20 minutes additional photosynthesis in air. The low endogenous sucrose in the leaf coupled with the improved tracer yield effected by the displacement technique gave sucrose with high specific activity. This sucrose-C14, hydrolyzed by 1% invertase, was a good source for radioactive glucose and fructose. Paper chromatographic procedures were used for the isolation and purification of the sugars.

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THE PREPARATION OF SUCROSE-C14 WITH HIGH SPECIFIC ACTIVITY AND HIGH TRACER YIELD USING DETACHED SUGAR BEET LEAVES

Canadian Journal of Biochemistry and Physiology ◽

10.1139/o59-021 ◽

1959 ◽

Vol 37 (2) ◽

pp. 193-197 ◽

Cited By ~ 3

Author(s):

C. D. Nelson ◽

D. C. Mortimer

Keyword(s):

Sugar Beet ◽

Specific Activity ◽

High Specific Activity ◽

Good Source ◽

Isolation And Purification

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Modified Method for the Preparation of Purified Bovine Prothrombin of High Specific Activity

Thrombosis and Haemostasis ◽

10.1055/s-0038-1651194 ◽

1968 ◽

Vol 19 (01/02) ◽

pp. 178-185 ◽

Cited By ~ 8

Author(s):

O. P Malhotra ◽

J. R Carter

Keyword(s):

Moving Boundary ◽

Specific Activity ◽

High Specific Activity ◽

Disc Electrophoresis ◽

Factor Vii ◽

Voltage Gradient ◽

Factor V ◽

Isolation And Purification ◽

Modified Method ◽

Very High

SummaryA modified method for the isolation and purification of bovine prothrombin is described. The preparations have a very high specific activity, viz. 3,200 ± 200 u/mg of protein, show a single symmetrical peak in the analytical ultracentrifuge and by moving boundary electrophoresis at both pH 6.86 and 8.6. They do not undergo inactivation or dissociation during electrophoresis at high voltage gradient (7.5) at alkaline pH. Disc electrophoresis also shows essentially a single component. For optimal activation, prothrombin requires the presence of factor VII-X complex in addition to factor V.

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Effects of Heparin Oligosaccharides with High Affinity for Antithrombin III in Experimental Venous Thrombosis

Thrombosis and Haemostasis ◽

10.1055/s-0038-1657178 ◽

1982 ◽

Vol 47 (03) ◽

pp. 244-248 ◽

Cited By ~ 47

Author(s):

D P Thomas ◽

Rosemary E Merton ◽

T W Barrowcliffe ◽

L Thunberg ◽

U Lindahl

Keyword(s):

Antithrombin Iii ◽

Specific Activity ◽

High Specific Activity ◽

Factor Xa ◽

Blood Levels ◽

Thrombin Time ◽

High Affinity ◽

Very High

SummaryThe in vitro and in vivo characteristics of two oligosaccharide heparin fragments have been compared to those of unfractionated mucosal heparin. A decasaccharide fragment had essentially no activity by APTT or calcium thrombin time assays in vitro, but possessed very high specific activity by anti-Factor Xa assays. When injected into rabbits at doses of up to 80 ¼g/kg, this fragment was relatively ineffective in impairing stasis thrombosis despite producing high blood levels by anti-Xa assays. A 16-18 monosaccharide fragment had even higher specific activity (almost 2000 iu/mg) by chromogenic substrate anti-Xa assay, with minimal activity by APTT. When injected in vivo, this fragment gave low blood levels by APTT, very high anti-Xa levels, and was more effective in preventing thrombosis than the decasaccharide fragment. However, in comparison with unfractionated heparin, the 16-18 monosaccharide fragment was only partially effective in preventing thrombosis, despite producing much higher blood levels by anti-Xa assays.It is concluded that the high-affinity binding of a heparin fragment to antithrombin III does not by itself impair venous thrombogenesis, and that the anti-Factor Xa activity of heparin is only a partial expression of its therapeutic potential.

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Autoprothrombin C Activity from Prothrombin with Snake Venom or Trypsin

Thrombosis and Haemostasis ◽

10.1055/s-0038-1655440 ◽

1962 ◽

Vol 08 (03) ◽

pp. 425-433 ◽

Cited By ~ 1

Author(s):

Ewa Marciniak ◽

Edmond R Cole ◽

Walter H Seegers

Keyword(s):

Snake Venom ◽

Thrombolytic Agent ◽

Sodium Citrate ◽

Specific Activity ◽

High Specific Activity ◽

Citrate Solution ◽

Clotting Factors ◽

Activation Products ◽

Russell’S Viper ◽

Autoprothrombin C

SummarySuitable conditions were found for the generation of autoprothrombin C from purified prothrombin with the use of Russell’s viper venom or trypsin. DEAE chromatographed prothrombin is structurally altered and has never been found to yield autoprothrombin C and also did not yield it when Russell’s viper venom or trypsin were used. Autoprothrombin C is derived from prothrombin with tissue extract thromboplastin, but not in large amounts with the intrinsic clotting factors. With the latter thrombin and autoprothrombin III are the chief activation products. Autoprothrombin III concentrates were prepared from serum and upon activation with 25% sodium citrate solution or with Russell’s viper venom large amounts of autoprothrombin C were obtained, and this was of high specific activity. Theoretically trypsin is not a thrombolytic agent, but on the contrary should lead to intravascular clotting.

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