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Results 1 - 5 of 5
EC Number
General Stability
highly purified ECGase II loses activity due to instability following purification
stable to repeated freezing and thawing
the stability of EGCII is markedly enhanced by formation of covalent complexes with cyclophellitol activity-based probes substituted with hydrophobic moieties, as evidenced by an increased melting temperature, resistance against tryptic digestion, changes in 15N-1H transverse relaxation optimized spectroscopy spectra of the [15N]Leu-labeled enzyme, and relative hydrophobicity as determined by 8-anilino-1-naphthalenesulfonic acid fluorescence. The stabilization of EGCII conformation correlates with the shape and hydrophobicity of the substituents of the activity-based probes
unstable at protein concentration below 0.2 mg/ml or without Triton X-100
unstable to repeated freezing and thawing
Results 1 - 5 of 5