Review of cyclotron production and quality control of “High specific activity” radionuclides for biomedical, biological, industrial and environmental applications at INFN-LASA

2001 ◽  
Author(s):  
C. Birattari
Keyword(s):  
Quality Control ◽  
Specific Activity ◽  
High Specific Activity ◽  
Environmental Applications ◽  
Cyclotron Production

Analytical and radioanalytical quality control in high specific activity radiotracer preparation

1995 ◽  
Vol 193 (1) ◽  
pp. 39-47 ◽  
Author(s):  
M. Gallorini ◽  
M. Bonardi ◽  
C. Birattari ◽  
F. Groppi ◽  
S. Saponaro
Keyword(s):  
Quality Control ◽  
Specific Activity ◽  
High Specific Activity

Radiochlorine: an underutilized halogen tool

2019 ◽  
Vol 107 (9-11) ◽  
pp. 1027-1031 ◽  
Author(s):  
Suzanne E. Lapi ◽  
Jonathan W. Engle
Keyword(s):  
Specific Activity ◽  
Research Effort ◽  
High Specific Activity ◽  
Low Energy ◽  
Emission Tomography ◽  
Clinical Settings ◽  
Cyclotron Production ◽  
Positron Emission ◽  
Chemistry Development ◽  
Fundamental Research

Abstract Halogen radioisotopes have a variety of physical half-lives which are suitable for probing a wide variety of pharmacokinetic processes. Compared with other radiohalogens, relatively little work has been done with radiochlorine. However, high specific activity radioisotopes of chlorine are available from low energy cyclotron production in quantities suitable for positron emission tomography (PET) and fundamental research. In particular, the sole radioisotope of chlorine which may be used for PET imaging, 34mCl, has achieved a state of development that permits imaging in clinical settings though sparse research effort has been focused on this isotope over the last 40 years. Additionally, the other longer-lived radioisotopes of chlorine will likely continue to show utility for more traditional radiotracer studies and chemistry development.

scholarly journals Cyclotron Production of High–Specific Activity 55 Co and In Vivo Evaluation of the Stability of 55 Co Metal-Chelate-Peptide Complexes

2015 ◽  
Vol 14 (10) ◽  
pp. 7290.2015.00025 ◽  
Author(s):  
Tara Mastren ◽  
Bernadette V. Marquez ◽  
Deborah E. Sultan ◽  
Elizabeth Bollinger ◽  
Paul Eisenbeis ◽  
...  
Keyword(s):  
Specific Activity ◽  
Metal Chelate ◽  
High Specific Activity ◽  
In Vivo Evaluation ◽  
Cyclotron Production ◽  
Peptide Complexes ◽  
The Stability

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

1982 ◽  
Vol 47 (03) ◽  
pp. 244-248 ◽  
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.

Autoprothrombin C Activity from Prothrombin with Snake Venom or Trypsin

1962 ◽  
Vol 08 (03) ◽  
pp. 425-433 ◽  
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.

In-Canal Assay of High Specific Activity 60Co at the Advanced Test Reactor

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