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• W2012659621 abstract "GroESLx proteins of symbiotic X‐bacteria were overproduced in Escherichia coli and their structural characteristics were assayed after simple purification. The GroESx and GroELx were heat‐stable at 80°C and 50°C, respectively. After heat‐treatment, GroESx was purified by DEAE Sephadex A‐50 chromatography and GroELx was purified by step‐ and linear sucrose density gradient ultracentrifugation. Molecular masses of GroESx and GroELx were 50–80 kDa and 800 kDa, respectively, as estimated by sucrose density gradient ultracentrifugation. In chemical cross‐linking analysis, subunits of GroESx were mostly cross‐linked by incubation for 3 h in 0.4% glutaraldehyde and GroESx was found to be composed of homo‐heptamer subunits. Those of GroELx were cross‐linked within 10 min in 0.3% glutaraldehyde and GroELx was in two stacks of homo‐heptamer subunits. On the other hand, GroESx and GroELx proteins in a solution could not be cross‐linked even after incubation for 3 h in 0.5% glutaraldehyde. GroELx was stable at 4–3713. In the presence of both GroESx and ATP, GroELx14 was stable at 3713 but not at 4°C or 2413. Thus, we confirmed the oligomeric properties of GroESx7 and GroELx14 and their stability to heat and in the interaction with GroESx." @default.
• W2012659621 created "2016-06-24" @default.
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• W2012659621 date "2002-01-01" @default.
• W2012659621 modified "2023-09-23" @default.
• W2012659621 title "Oligomeric characterization of GroESIx Chaperonin from symbiotic X‐Bacteria inAmoeba proteus" @default.
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• W2012659621 doi "https://doi.org/10.1080/12265071.2002.9647656" @default.
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