scholarly journals Managing a High Specific Activity Iobenguane Therapy Clinic: From Operations to Reimbursement

2021 ◽  
pp. jnumed.121.262306
Author(s):  
Sophia O'Brien ◽  
Daniel A Pryma
1982 ◽  
Vol 47 (03) ◽  
pp. 244-248 ◽  
Author(s):  
D P Thomas ◽  
Rosemary E Merton ◽  
T W Barrowcliffe ◽  
L Thunberg ◽  
U Lindahl

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.


1962 ◽  
Vol 08 (03) ◽  
pp. 425-433 ◽  
Author(s):  
Ewa Marciniak ◽  
Edmond R Cole ◽  
Walter H Seegers

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.


2021 ◽  
pp. 1-7
Author(s):  
Michael A. Reichenberger ◽  
Jagoda M. Urban-Klaehn ◽  
Jason V. Brookman ◽  
Joshua L. Peterson-Droogh ◽  
Jorge Navarro ◽  
...  

1964 ◽  
Vol 239 (11) ◽  
pp. 3743-3748 ◽  
Author(s):  
Joseph L. Izzo ◽  
William F. Bale ◽  
Mary Jane Izzo ◽  
Angela Roncone

Biochemistry ◽  
1997 ◽  
Vol 36 (7) ◽  
pp. 1943-1952 ◽  
Author(s):  
Alexandra Koschak ◽  
Robert O. Koch ◽  
Jessica Liu ◽  
Gregory J. Kaczorowski ◽  
Peter H. Reinhart ◽  
...  

1979 ◽  
Vol 17 (1) ◽  
pp. 55-59
Author(s):  
T.J. Gillespie ◽  
R.L. Price

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