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Isolation of a teratocarcinoma stem cell lectin implicated in intercellular adhesion
FEBS Letters
|April 22, 1985
Summary
Researchers purified a stem cell lectin, a protein that binds carbohydrates, from teratocarcinoma stem cells. This lectin, with a molecular weight of 56-kDa, shows specific binding to fucans and mannans.
Area of Science:
- Biochemistry
- Molecular Biology
- Stem Cell Research
Background:
- A cell surface lectin from teratocarcinoma stem cells with fucan/mannan specificity was previously identified.
- Lectins play crucial roles in cellular recognition and adhesion, particularly in stem cell biology.
Purpose of the Study:
- To purify and characterize the hemagglutinin (lectin) from teratocarcinoma stem cell conditioned medium.
- To identify the specific polypeptide responsible for the lectin's hemagglutination activity.
Main Methods:
- Purification using Sepharose 2B column chromatography and DEAE-cellulose ion-exchange chromatography.
- Analysis of purified material by SDS-polyacrylamide gel electrophoresis (SDS-PAGE).
- Renaturation of hemagglutination activity from gels and localization via fluorography.
Main Results:
- Achieved an approximate 90-fold purification of the hemagglutinin.
- SDS-PAGE revealed a major polypeptide band with a molecular weight of 56,000 (56-kDa).
- Hemagglutination activity was localized exclusively to the 56-kDa component after renaturation.
Conclusions:
- The purified 56-kDa polypeptide is identified as the lectin responsible for hemagglutination.
- This finding contributes to understanding the molecular components of teratocarcinoma stem cell surface interactions.