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- W2094788765 abstract "Abstract Brief treatment of hepatoma cells in monolayer culture with concanavalin A causes a decrease in tyrosine aminotransferase specific activity that is thought to be a rapid, reversible inactivation of the enzyme (T.V. Gopalakrishnam and E.B. Thompson 1977 J. Biol. Chem. 252 , 2717–2725). We confirm this decrease, but attribute it to an increased leakage of cellular protein from concanavalin A-treated monolayer cultures during the harvesting procedure. If the cells are washed free of medium and lysed in , situ by freezing and thawing them, or by treating them with buffer containing a nonionic detergent, equal amounts of tyrosine aminotransferase are found in concanavalin A-treated and untreated cells. If cells are harvested by scraping them from the substrate, some tyrosine aminotransferase is lost into the buffer used to collect the cells. Treatment of cells with concanavalin A markedly increases the amount of enzyme lost during this procedure, and results in a low enzyme content in the washed cells. No inactivation occurs, however, because the total amount of tyrosine aminotransferase present in the cell pellet and the wash buffer is equal for treated and untreated cells." @default.
- W2094788765 created "2016-06-24" @default.
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- W2094788765 date "1982-06-01" @default.
- W2094788765 modified "2023-09-23" @default.
- W2094788765 title "Explanation for the apparent inactivation of tyrosine aminotransferase in hepatoma cells by concanavalin A" @default.
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- W2094788765 doi "https://doi.org/10.1016/0006-291x(82)91816-2" @default.
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