000 01402 a2200385 4500
005 20250513054243.0
264 0 _c19940714
008 199407s 0 0 eng d
022 _a0006-291X
024 7 _a10.1006/bbrc.1994.1781
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aRoth, N J
245 0 0 _aSite directed substitutions suggest that His-418 of beta-galactosidase (E. coli) is a ligand to Mg2+.
_h[electronic resource]
260 _bBiochemical and biophysical research communications
_cJun 1994
300 _a866-70 p.
_bdigital
500 _aPublication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
650 0 4 _aAmino Acid Sequence
650 0 4 _aBase Sequence
650 0 4 _aBinding Sites
650 0 4 _aDNA Primers
650 0 4 _aEscherichia coli
_xenzymology
650 0 4 _aHistidine
650 0 4 _aHydrogen-Ion Concentration
650 0 4 _aKinetics
650 0 4 _aLigands
650 0 4 _aMagnesium
_xmetabolism
650 0 4 _aMolecular Sequence Data
650 0 4 _aMutagenesis, Site-Directed
650 0 4 _aPoint Mutation
650 0 4 _aRecombinant Proteins
_xbiosynthesis
650 0 4 _abeta-Galactosidase
_xbiosynthesis
700 1 _aHuber, R E
773 0 _tBiochemical and biophysical research communications
_gvol. 201
_gno. 2
_gp. 866-70
856 4 0 _uhttps://doi.org/10.1006/bbrc.1994.1781
_zAvailable from publisher's website
999 _c8002351
_d8002351