@article {16623,
	title = {Dimerization of Thermomonospora fusca beta-1,4-endoglucanase E2},
	journal = {Biochemistry},
	volume = {32},
	year = {1993},
	note = {DA - 19930916
IS - 0006-2960 (Print)
IS - 0006-2960 (Linking)
LA - eng
PT - Journal Article
PT - Research Support, U.S. Gov{\textquoteright}t, Non-P.H.S
RN - 0 (Cross-Linking Reagents)
RN - 0 (Disulfides)
RN - EC 3.2.1.4 (Cellulase)
RN - T3C89M417N (Glutaral)
SB - IM},
	month = {1993/08/17/},
	pages = {8146 - 8150},
	abstract = {Unboiled Thermomonospora fusca endoglucanase E2 electrophoresed on SDS-polyacrylamide gels migrated in the range of 80-90 kDa, but when boiled it migrated in the 40-42-kDa range. Sedimentation equilibrium centrifugation as well as chemical cross-linking experiments confirmed that E2 is a dimer. The dimer was reversibly dissociated at low pH. The E2 dimer was stable up to 70 degrees C, but began to dissociate at this temperature after a 30-60-min incubation. A nondimerizing mutant was obtained using region-specific chemical mutagenesis. DNA sequencing of this mutant revealed a single base change that substituted Gly for Glu-263. Chemical modification of carboxylic acid residues in E2 disrupted the dimer interaction},
	keywords = {Actinomycetales, Blotting,Western, Cellulase, chemistry, Cross-Linking Reagents, Disulfides, Electrophoresis,Polyacrylamide Gel, Enzyme Stability, enzymology, Glutaral, Hot Temperature, Hydrogen-Ion Concentration, metabolism, Molecular Weight, Mutation, Oxidation-Reduction, Ultracentrifugation},
	url = {PM:8347613},
	author = {McGinnis,K. and Kroupis, C. and Wilson,D.B.}
}
