3.2.1.123	highly purified ECGase II loses activity due to instability following purification	646690	
3.2.1.123	stable to repeated freezing and thawing	646688	
3.2.1.123	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	749905	
3.2.1.123	unstable at protein concentration below 0.2 mg/ml or without Triton X-100	646691	
3.2.1.123	unstable to repeated freezing and thawing	646691