These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: [Study on binding characteristics of 125I-labeled McAb LC-1 to lung adenocarcinoma cells in vitro and in vivo].
    Author: Li M, Lian BJ, Ge XR.
    Journal: Shi Yan Sheng Wu Xue Bao; 1992 Mar; 25(1):31-8. PubMed ID: 1598801.
    Abstract:
    McAb LC-1 was derived from fusion of myeloma cells and murine spleen cells immunized with human lung adenocarcinoma SPC-A-1 cells. The immunoglobulin isotype of LC-1 belonged to IgM. LC-1 was direct against the common epitope of lung cancer. It not only reacted with small cell lung cancer but also with non small cell lung cancer. LC-1 was purified from ascitic fluid by euglobulin precipitation and Sephadex G-200 filtration chromatography, and was iodinated with Iodogen, the specific reactivity of 125I-labeled LC-1 was determined by comparing standard curve with self-displacement curve. The immunoreactive fraction of 125I-LC-1 was determined by its binding to excess of antigen. The RIA data were plotted in Scatchard-form as binding of SPC-A-1 cells to LC-1. The binding constant of LC-1 binding to SPC-A-1 was 4.8 x 10(8) M-1. The LC-1 binding sites on SPC-A-1 were 7.2 x 10(4) per cell. The RIA inhibition test showed that LC-1 and LAC-122 (another IgM isotype McAb reacted only with non small cell lung cancer) had no cross-reactivity. The treatment of SPC-A-1 cells by proteinase and sodium periodate inhibited LC-1 binding to these treated target cells by 39% and 66% respectively. These results suggested that the biochemical nature of antigen recognized by LC-1 was glycoprotein.(ABSTRACT TRUNCATED AT 250 WORDS)
    [Abstract] [Full Text] [Related] [New Search]