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• W1565856959 abstract "Abstract Matrix-bound (MB) subunits of aldolase were prepared by attaching tetrameric aldolase to Sepharose and removing those subunits not covalently linked to Sepharose. Comparison of the protein contents of the MB-derivatives leads to the conclusion that under the conditions used, most molecules of aldolase were attached covalently via only one subunit. The properties of MB-subunit aldolase were compared with those of the corresponding matrix-bound tetrameric enzyme (MB-aldolase). MB-subunit aldolase is more sensitive to inactivation by alkali and loses more than half its activity at pH 9.7. In contrast, MB-aldolase begins to be inactivated only at pH 10.5. The differences in stability between the monomeric and tetrameric forms of aldolase towards alkali explains why native aldolase is stable and active at pH 10 whereas dissociated aldolase does not regenerate activity at this pH. Differences between MB-aldolase and MB-subunit aldolase in heat stability and susceptibility to proteolytic inactivation were also observed. These differences, together with results reported earlier suggest the presence of spatially separated monomers in MB-subunit aldolase. The Michaelis constants for fructose-1,6-diphosphate and fructose-1-phosphate are similar for both MB-aldolase and MB-subunit aldolase. There is also no difference in the ratio of the reaction velocities for these two substrates or the activation energy for the fructose diphosphate cleavage reaction. The values of all these constants are close to those for the free enzyme in solution. A discontinuity in the Arrhenius plot was found for both MB-derivatives. It appears that subunit interactions confer stability on the tetrameric form of aldolase but have little or no effect on several of its catalytic properties." @default.
• W1565856959 created "2016-06-24" @default.
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• W1565856959 date "1972-03-01" @default.
• W1565856959 modified "2023-09-28" @default.
• W1565856959 title "Studies on protein subunits" @default.
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• W1565856959 doi "https://doi.org/10.1016/0003-9861(72)90307-4" @default.
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