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Results: 1-19 |
Results: 19

Authors: GALLAGHER CN HUBER RE
Citation: Cn. Gallagher et Re. Huber, STUDIES OF THE M15 BETA-GALACTOSIDASE COMPLEMENTATION PROCESS, Journal of protein chemistry, 17(2), 1998, pp. 131-141

Authors: ROTH NJ ROB B HUBER RE
Citation: Nj. Roth et al., HIS-357 OF BETA-GALACTOSIDASE (ESCHERICHIA-COLI) INTERACTS WITH THE C3 HYDROXYL IN THE TRANSITION-STATE AND HELPS TO MEDIATE CATALYSIS, Biochemistry, 37(28), 1998, pp. 10099-10107

Authors: ROB B ROTH NJ HUBER RE
Citation: B. Rob et al., HIS-357, AN IMPORTANT RESIDUE IN BETA-GALACTOSIDASE (ESCHERICHIA-COLI) FOR BINDING GALACTOSYL TRANSITION-STATE ANALOGS, The FASEB journal, 11(9), 1997, pp. 1728-1728

Authors: GALLAGHER CN HUBER RE
Citation: Cn. Gallagher et Re. Huber, MONOMER-DIMER EQUILIBRIUM OF UNCOMPLEMENTED M15 BETA-GALACTOSIDASE FROM ESCHERICHIA-COLI, Biochemistry, 36(6), 1997, pp. 1281-1286

Authors: MARTINEZBILBAO M HUBER RE
Citation: M. Martinezbilbao et Re. Huber, THE ACTIVATION OF BETA-GALACTOSIDASE (ESCHERICHIA-COLI) BY MG2+ AT LOWER PH VALUES, Biochemistry and cell biology, 74(2), 1996, pp. 295-298

Authors: HUBER RE ROTH NJ BAHL H
Citation: Re. Huber et al., QUATERNARY STRUCTURE, MG2-PROPERTIES OF THE BETA-GALACTOSIDASE FROM THERMOANAEROBACTERIUM THERMOSULFURIGENES EM1( INTERACTIONS, AND SOME KINETIC), Journal of protein chemistry, 15(7), 1996, pp. 621-629

Authors: RICHARD JP HUBER RE LIN S HEO C AMYES TL
Citation: Jp. Richard et al., STRUCTURE-REACTIVITY RELATIONSHIPS FOR BETA-GALACTOSIDASE (ESCHERICHIA-COLI, LAC-Z) .3. EVIDENCE THAT GLU-461 PARTICIPATES IN BRONSTED ACID-BASE CATALYSIS OF BETA-D-GALACTOPYRANOSYL GROUP-TRANSFER, Biochemistry, 35(38), 1996, pp. 12377-12386

Authors: RICHARD JP HUBER RE HEO C AMYES TL LIN S
Citation: Jp. Richard et al., STRUCTURE-REACTIVITY RELATIONSHIPS FOR BETA-GLACTOSIDASE (ESCHERICHIA-COLI, LAC Z) .4. MECHANISM FOR REACTION OF NUCLEOPHILES WITH THE GALACTOSYL-ENZYME INTERMEDIATES OF E461G AND E461Q BETA-GALACTOSIDASES, Biochemistry, 35(38), 1996, pp. 12387-12401

Authors: ROTH NJ HUBER RE
Citation: Nj. Roth et Re. Huber, GLU-416 OF BETA-GALACTOSIDASE (ESCHERICHIA-COLI) IS A MG2-GALACTOSIDASES WITH SUBSTITUTIONS FOR GLU-416 ARE INACTIVATED, RATHER THAN ACTIVATED, BY MG2+( LIGAND AND BETA), Biochemical and biophysical research communications, 219(1), 1996, pp. 111-115

Authors: MARTINEZBILBAO M GAUNT MT HUBER RE
Citation: M. Martinezbilbao et al., E461H-BETA-GALACTOSIDASE (ESCHERICHIA-COLI) - ALTERED DIVALENT METAL SPECIFICITY AND SLOW BUT REVERSIBLE METAL INACTIVATION, Biochemistry, 34(41), 1995, pp. 13437-13442

Authors: ROTH NJ HUBER RE
Citation: Nj. Roth et Re. Huber, INVESTIGATION OF THE MAGNESIUM BINDING-SITE OF BETA-GALACTOSIDASE (ESCHERICHIA-COLI), The FASEB journal, 8(7), 1994, pp. 10001344-10001344

Authors: GALLAGHER CN HUBER RE
Citation: Cn. Gallagher et Re. Huber, STABILITY OF M15 BETA-GALACTOSIDASE UNDER CONDITIONS WHICH AFFECT TETRAMERIZATION (ALPHA-COMPLEMENTATION), The FASEB journal, 8(7), 1994, pp. 10001387-10001387

Authors: MARTINEZBILBAO M HUBER RE
Citation: M. Martinezbilbao et Re. Huber, SUBSTITUTIONS FOR GLY-794 SHOW THAT BINDING INTERACTIONS ARE IMPORTANT DETERMINANTS OF THE CATALYTIC ACTION OF BETA-GALACTOSIDASE (ESCHERICHIA-COLI), Biochemistry and cell biology, 72(7-8), 1994, pp. 313-319

Authors: YUAN JM MARTINEZBILBAO M HUBER RE
Citation: Jm. Yuan et al., SUBSTITUTIONS FOR GLU-537 OF BETA-GALACTOSIDASE FROM ESCHERICHIA-COLICAUSE LARGE DECREASES IN CATALYTIC ACTIVITY, Biochemical journal, 299, 1994, pp. 527-531

Authors: GALLAGHER CN ROTH NJ HUBER RE
Citation: Cn. Gallagher et al., A RAPID METHOD FOR THE PURIFICATION OF LARGE AMOUNTS OF AN ALPHA-COMPLEMENTING PEPTIDE DERIVED FROM BETA-GALACTOSIDASE (ESCHERICHIA-COLI), Preparative biochemistry, 24(3-4), 1994, pp. 297-304

Authors: HUBER RE GUPTA MN KHARE SK
Citation: Re. Huber et al., THE ACTIVE-SITE AND MECHANISM OF THE BETA-GALACTOSIDASE FROM ESCHERICHIA-COLI, International Journal of Biochemistry, 26(3), 1994, pp. 309-318

Authors: ROTH NJ HUBER RE
Citation: Nj. Roth et Re. Huber, SITE-DIRECTED SUBSTITUTIONS SUGGEST THAT HIS-418 OF BETA-GALACTOSIDASE (ESCHERICHIA-COLI) IS A LIGAND TO MG2+, Biochemical and biophysical research communications, 201(2), 1994, pp. 866-870

Authors: RING M HUBER RE
Citation: M. Ring et Re. Huber, THE PROPERTIES OF BETA-GALACTOSIDASES (ESCHERICHIA-COLI) WITH HALOGENATED TYROSINES, Biochemistry and cell biology, 71(3-4), 1993, pp. 127-132

Authors: HUBER RE CHIVERS PT
Citation: Re. Huber et Pt. Chivers, BETA-GALACTOSIDASES OF ESCHERICHIA-COLI WITH SUBSTITUTIONS FOR GLU-461 CAN BE ACTIVATED BY NUCLEOPHILES AND CAN FORM BETA-D-GALACTOSYL ADDUCTS, Carbohydrate research, 250(1), 1993, pp. 9-18
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