Escherichia coli P-galactosidase

Geller AI, Breakefield XO (1988) A defective HSV-1 vector expresses Escherichia coli p-galactosidase in cultured peripheral neurons. Science 241 1667—1669. 

The first demonstrated example of enzyme induction came from studies conducted in the 1950s on the bacterium Escherichia coli. p-galactosidase, an enzyme required for the utilization of lactose, catalyzes the hydrolysis of lactose to D-galactose and o-glucose. 

Escherichia coli P-galactosidase antibody rabbit IgG (1° antibody Chemicon International Ltd. Temecula CA, AB1211-5MG). 

P3. Pisetsky, D. S., and Grudier, J. P., Polyspecific binding of Escherichia coli beta-galactosidase by murine antibodies to DNA. J. Immunol. 143,3609—3613 (1989). 

Clemmit, R.H. and Chase, H.A., Immobilized metal affinity chromatography of P-galactosidase from unclarified Escherichia coli homogenates using expanded bed adsorption, /. Chromatogr. A, 874, 27, 2000. 

Commercially available P-gal usually is isolated from Escherichia coli and has a pH optimum at 1-1.5. By contrast, mammalian p-galactosidases usually have a pH optimum within the range of 5.5-6 thus, interference from endogenous P-gal during immunohistochemical staining can be avoided. 

Detection of one molecule of P-D-galactosidase produced from Escherichia coli 152 Bovine serum albumin increases initial light intensity and eliminates the ad- 153... 

Escherichia coli cells grown in a medium with lactose as the only carbon source are monitored for p-galactosidase activity over time with the results shown below. 

B. W. Bainbridge, N. Mathias, R. G. Price, A. C. Richardson, J. Sandhu, and B. V. Smith, Improved methods for the detection of P-galactosidase activity in colonies of Escherichia coli using a new chromogenic substrate VBzTM-gal (2-[2-(4-P-D-galactopyranosyl-3-methoxyphenyl)-vinyl]-3-methyl-benzothiazolium toluene- 4-sulphonate), FEMS Microbiol. Lett., 80 (1991) 319-324. 

J. D. McCarter, M. J. Adam, and S. G. Withers, Binding energy and catalysis. Fluorinated and deoxygen-ated glycosides as mechanistic probes of Escherichia coli (lac Z) p-galactosidase, Biochem. J., 286 (1992) 721-727. 

M. L. Sinnot and P. J. Smith, Affinity labelling with deaminatively generated carbonium ion. Kinetics and stoicheiometry of die alkylation of methionine-500 of die lacZ p-galactosidase of Escherichia coli by p-D-galactopyranosylmethyl-p-nitrophenyltriazene, Biochem. J., 175 (1978) 525—538. 

J. Langridge, Mutations conferring quantitative and qualitative increases in P-galactosidase activity in Escherichia coli, Mol. Gen. Genet., 105 (1969) 74-83. 

S. Yoon, H.G. Kim, K.H. Chun, J.E.N. Shin, 4-deoxy-analogs of p-nitrophenyl /i-D-galactopyranosides for specificity study with /J-galactosidase from escherichia coli. Bull. Korean Chem. Soc. 17 (1996) 599-604. 

J.P. Richard, J.G. Westerfeld, S. Lin, Structure-reactivity relationships for beta-galactosidase (Escherichia coli, lac Z). 1. Bronsted parameters for cleavage of alkyl beta-D-galactopyranosides, Biochemistry 34 (1995) 11703-11712. 

Hamaguchi, Y., Yoshitake, S., Ishikawa, E., Endo, Y., and Ohtaki, S. (1979) Improved procedure for the conjugation of rabbit IgG and Fab antibodies with p-D-galactosidase from Escherichia coli using N,N -o-phenylenedimaleimide./. Biochem. (Tokyo) 85,1289—1300. 

Deoxygenation of the partially substituted lactoside derivative 3694 was accomplished by the Barton reduction method to afford the 4 -dcoxy-p-lactosidc 37.6 The 4 -deoxy derivative was not a substrate for the p-D-galactosidase (E.C. 3.2.1.23) of Escherichia coli. 

Tocaj, A., Nandakumar, M. P., Holst, O., and Mattiasson, B. (1999). Flow injection analysis of intracellular /3-galactosidase in Escherichia coli cultivations, using an on-line system including cell disruption, debris separation and immunochemical quantification. Bioseparation 8, 255-267. 

E. Steers, P. Cuatrecasas, and H. B. Pollard, J. Biol. Chem. 246 196 (1971). The Purification of (S-Galactosidase from Escherichia coli by Affinity Chromatography. 

J. P. Richard, D. A. McCall, C. K. Heo, and M. M. Toteva, Ground-state, transitions-state, and metal-cation effects of the 2-hydroxy group onjd-D-galactopyranosyl transfer catalyzed by j6-galactosidase (Escherichia coli, lac Z), Biochemistry, 44 (2005) 11872-11881. 

In general, hydrophobic cationic compounds are the preferred but not only substrates of MFS MDRs. MdfA from Escherichia coli [54] can extrude neutral compounds such as chloramphenicol in addition to various cationic compounds. MdfA was also shown to pump out an artificial substrate of P-galactosidase, isopropyl-P-o-galactoside [55]. 

---