Preparation of ^<99m>Tc radiopharmaceuticals using macroreticular Sn (II) complex
| Project/Area Number |
04557104
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| Research Category |
Grant-in-Aid for Developmental Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Physical pharmacy
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| Research Institution | Kumamoto University |
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Principal Investigator |
NAKAYAMA Morio Kumamoto University, Pharmaceutical Sciences, Associate Professor, 薬学部, 助教授 (60164373)
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| Co-Investigator(Kenkyū-buntansha) |
YOMOTA Isamu Daiichi Radioisotope Laboratories, Reseracher, 研究開発部, 研究員
TOMIGUCHI Seiji Kumamoto University, Pharmaceutical Sciences, Lecturerer, 医学部附属病院, 講師 (20172182)
HARADA Kumiko Kumamoto University, Pharmaceutical Sciences, Assistant Professor, 薬学部, 助手 (70150547)
杉井 篤 熊本大学, 薬学部, 教授 (40040323)
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| Project Period (FY) |
1992 – 1994
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| Project Status |
Completed (Fiscal Year 1994)
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| Budget Amount *help |
¥2,900,000 (Direct Cost: ¥2,900,000)
Fiscal Year 1994: ¥300,000 (Direct Cost: ¥300,000)
Fiscal Year 1993: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1992: ¥2,000,000 (Direct Cost: ¥2,000,000)
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| Keywords | Technetium / Macromolecular Sn (II) complex / Aminophosphonic acid groups / Monoclonal anitibody / Immunoglobulin / アルブミン / キレート樹脂 |
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| Research Abstract |
Stannous chloride (SnCl_2) has the disadvantages of being easily hydrolyzed and oxidized, but it is included in most commercial kits as an appropriate reducing agent in the preparation of ^<99m>Tc radiopharmaceuticals. The replacement of SnCl_2 by the insoluble macromolecular Sn (II) (R-Sn) complex was proposed as a way to resolve some of the problems caused by a large excess of SnCl_2 Macroreticular chelating ion exchange resins having an adsorption ability for Sn (II) were investigated for the development of R-Sn complex. Among them, a chelating resin containing aminophosphonic acid groups showed a high capacity for Sn (II) , which bound strongly to the resin by chelation. The use of the R-Sn complex was expected to minimize Sn (II) comtamination of the ^<99m>Tc labeling solution and be effectively used as a reducing agent for ^<99m>Tc labeling of proteins containing sulfhydryl groups. So, the R-Sn complex was applied to the direct ^<99m>Tc labeling of human immunoglobulin (IgG) to minimize the influence of Sn (II). ^<99m>Tc labeling was achieved at greater than 90% yield simply by the short-term mixing of IgGa containing>2 -SH groups per IgG molecule, ^<99m>Tc pertechnetate, and the R-Sn complex in pH 7 solution. The ^<99m>Tc-IgGa obtained by this labeling method has high stability based on the thiol-specific binding of ^<99m>Tc without transchelation from another weakly bound ^<99m>Tc-complex.
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Report
(4 results)
Research Products
(12 results)
