<sup>103</sup>Ruの腫瘍親和性

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書誌事項

タイトル別名
  • <sup>103</sup>Ru for Tumor Scanning
  • 103Ruの腫瘍親和性-2-ルテニウムのがん細胞結合機構の解析
  • 103Ru ノ シュヨウ シンワセイ 2 ルテニウム ノ ガン サイボウ ケツ
  • 第2編 ルテニウムのがん細胞結合機構の解析
  • Part II. The mechanism of ruthenium binding to tumor cells

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抄録

The mechanism of 103Ru-uptake in tumors was investigated through the incubation of rat ascites hepatoma cells (AH-130) in vitro with various concentrations of Ru-chloride containing 103Ru-chloride as a tracer. Quantitative analysis of Ru binding to the cells indicated that ascites hepatoma cells contained high- and low-affinity binding sites for Ru. When ascites hepatoma cells were incubated with Ru after incubation with a low concentration of papain, most of the Ru was not bound to the cells but was found in the medium containing solubilized glycoproteins. However Ru bound mainly to washed cells after the incubation with papain. About 65% of the Ru bound to ascites hepatoma cells was liberated by the papain treatment, and about 45% of the liberated Ru was precipitated by cetyltrimethylammonium bromide, indicating that Ru bound tightly to glycopeptides. These results suggest that the tumor affinity of 103Ru is related to specific binding to glycopeptides on the tumor cell surface.

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