Steps toward High Specific Activity Labeling of Biomolecules for Therapeutic Application:  Preparation of Precursor [188Re(H2O)3(CO)3]+and Synthesis of Tailor-Made Bifunctional Ligand Systems

2002 ◽  
Vol 13 (4) ◽  
pp. 750-756 ◽  
Author(s):  
Roger Schibli ◽  
Rolf Schwarzbach ◽  
Roger Alberto ◽  
Kirstin Ortner ◽  
Helmut Schmalle ◽  
...  
Keyword(s):  
Specific Activity ◽  
High Specific Activity ◽  
Therapeutic Application ◽  
Bifunctional Ligand

scholarly journals Production and therapeutic application of rhenium isotopes, rhenium-186 and rhenium-188: Radioactive pharmaceuticals of the future

2003 ◽  
Vol 56 (7-8) ◽  
pp. 362-365 ◽  
Author(s):  
Jurij Vucina ◽  
Ruben Han
Keyword(s):  
Saline Solution ◽  
Specific Activity ◽  
Nuclear Reactors ◽  
High Specific Activity ◽  
Interventional Cardiology ◽  
Pain Palliation ◽  
Chemical Similarity ◽  
Therapeutic Application ◽  
Beta Emitters ◽  
Metallic Rhenium

Introduction In contemporary nuclear medicine, alpha, pure beta or beta-gamma emitters are used for targeted therapy. Use of pure and combined alpha/beta emitters in oncology, endocrinology, rheumatology and, a short while ago, interventional cardiology, has refined as an important alternative to more common therapeutic regimens. Two radioisotopes of rhenium, rhenium-186 and rhenium-188, are of particular interest. Production of Rhenium-186 and Rhenium-188 Rhenium-186 is routinely produced in nuclear reactors by direct neutron activation of metallic rhenium enriched with 185Re via 185Re(n,)186Re nuclear reaction. For production of 188Re the target is 186W. 188W is produced by double neutron capture which gives 188Re due to beta decay. Separation of 188Re is performed in generators by column chromatography, extraction or by gel technology. The best results are obtained using chromatographic 188W/188Re generator in which 188W is adsorbed on aluminum. Rhenium-188 is eluted in saline solution. Radiopharmaceuticals labeled with rhenium radioisotopes and their clinical applications There are several fields of applications of radiopharmaceuticals labeled with 186,188Re. For bone pain palliation the most often used are 186Re-HEDP and 188Re-DMSA. For synovectomy, 186Re-sulphide in kit form is already commercially available. Endovascular radiation therapy is performed by using 188Re-perrhenate or 188Re-MAG3. Labeling of peptides and antibodies with 188Re is also reported. Application of rhenium radioisotopes depends on their specific activity. Rhenium-186,188 of low specific activity can be used only for labeling of particles or diphosphonates. However, labeling of peptides or antibodies can be performed only by using 188Re of high specific activity. Conclusion 188Re is expected to have wide applications after development of a chromatographic 188W/188Re generator. One of the advantages of rhenium is its chemical similarity with technetium. So technetium analogues labeled with 186,188Re can be developed for several specific applications.

Very stable 188Re-S4 chelates for labelling biomolecules

2007 ◽  
Vol 46 (05) ◽  
pp. 181-184 ◽  
Author(s):  
C. Jentsche ◽  
R. Bergmann ◽  
H.-J. Pietzsch ◽  
G. Wunderlich ◽  
J. Kotzerke ◽  
...  
Keyword(s):  
Ascorbic Acid ◽  
Specific Activity ◽  
Direct Reduction ◽  
High Specific Activity ◽  
Amine Group ◽  
Stability Studies ◽  
Therapeutic Application ◽  
Carboxylic Groups

SummaryAim: The preparation and stability of a new 188Re-S4-complex [S4 = (1-aza-18-crown-6)(O)C-C(SH)-C(SH)- C(O)NH-(CH2)3-NH-(CH2)3-NHC(O)-C(SH)-C(SH)- C(O)(1-aza-18-crown-6] was studied at therapeutic relevant radioactive concentrations. The results were compared with 188Re-MAG3 (MAG3: mercaptoacetyltriglycine) and 188Re-DMSA preparations (DMSA: dimercaptosuccinic acid) performed with the same highly concentrated [188Re]perrhenate solution (12-15 GBq/ml). Methods: The 188Re complexes were prepared by direct reduction of perrhenate (188Re-S4-complex) as well as via the 188Re- EDTA precursor complex (188Re-MAG3, 188Re-DMSA). The preparations were stabilised with 15 mg of ascorbic acid and analysed after 1, 2, and 24 hours by TLC and HPLC. Additionally, in vitro and in vivo stability studies were performed with the purified complexes. Results: After stabilisation with 15 mg of ascorbic acid, all of the complexes were nearly stable under nitrogen for hours, and only 2–8 % of perrhenate was observed after 24 h. In contrast, only the 188Re-S4 complex was completely stable in vitro and in all investigated in vivo samples after separation of ligand excess and reducing agent by HPLC. Conclusion: The bridging amine group or free carboxylic groups of the S4-ligand framework make available reactive positions for coupling biomolecules to the chelate. Thus it appears that the new 188Re-S4 complexes offer the possibility of stable and high specific activity labelling of biomolecules for therapeutic application.

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

scholarly journals High Specific Activity Labeling of Insulin with 131I

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

[125I]Iberiotoxin-D19Y/Y36F, the First Selective, High Specific Activity Radioligand for High-Conductance Calcium-Activated Potassium Channels

Biochemistry ◽  
1997 ◽  
Vol 36 (7) ◽  
pp. 1943-1952 ◽  
Author(s):  
Alexandra Koschak ◽  
Robert O. Koch ◽  
Jessica Liu ◽  
Gregory J. Kaczorowski ◽  
Peter H. Reinhart ◽  
...  
Keyword(s):  
Potassium Channels ◽  
Specific Activity ◽  
High Specific Activity ◽  
Calcium Activated Potassium Channels ◽  
High Conductance
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