Of p-galactosidase

Husum et al. found that the hydrolytic activities of P-galactosidase from E. coli and the protease subtilisin in a 50 % aqueous solution of the water-miscible ionic liquid [BMIM][Bp4] were comparable to those in 50 % aqueous solutions of ethanol or acetonitrile (Entry 9) [37]. 

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. 

Farkade VD, Harrison STL, Pandit AB (2006) Improved cavitational cell disruption following pH pretreatment for the extraction of P-galactosidase from Kluveromyces lactis. Biochem Eng J 31 25-30... 

Galactosialidosis is characterized by the simultaneous deficiencies of P-galactosidase and a-neuroaminidase. Clinical and pathological manifestations resemble those in GM1 gangliosidosis and like it show a range of severity. The underlying defect involves a protective protein, which stabilizes these two enzymes by a mechanism that is not understood. Curiously, the protective protein is itself a peptidase. The disorder is most common in Japan. The defective gene has been cloned and mutations have been identified. 

MetPLATE Kit P-galactosidase activity E. coli, inhibition of p-galactosidase activity [19,40]... 

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. 

F. Naider, Z. Bohak, and J. Yariv, Reversible alkylation of a methionyl residue near die active site of p-galactosidase, Biochemistry, 11 (1972) 3202—3207. 

The characterization of the nar promoter in E. coli with the intact nar operon on the chromosome was carried out. Expression of P-galactosidase was maximal when the nar promoter was induced at ODgoo =1-7 under anaerobic conditions in the presence of 1 % nitrate. At this optimal condition the induction ratio was approximately 250 and the specific P-galactosidase activity was approximately 7500 Miller units at ODgoo = 2.7 [35]. In this study, we used plasmid... 

G. F. Herrmann, Y. Ichikawa, C. Wandtey, F. C. A. Gaeta, J. C. Paulson, and C.-H. Wong, A new multi-enzyme system for a one-pot synthesis of sialyl oligosaccharides Combined use of P-galactosidase and a(2,6)-sialyltransferase coupled with regeneration in situ of CMP-sialic acid, Tetrahedron Lett. 34 3091 (1993). 

Color Plate 14 Histochemical analysis of P -galactosidase gene expression in liver, 424... 

Fig. 7 Transfection of P-galactosidase by cholesterol-based amine derivatives at lipid/DNA ratio of 4 1 in mouse melanoma cells (B16F0) [37]...

Miller JH (1972), Assay of p-galactosidase, In Miller JH (Ed.), Experiments in Molecular Genetics, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, pp. 352-355. 

Eukaryotic genes may be clustered (for example, genes for a metabolic pathway may occur on the same region of a chromosome) but are independently controlled. Operons or polycistronic mRNAs do not exist in eukaryotes. This contrasts with prokaryotic genes, where a single control gene often acts on a whole cluster (for example, lac I controls the synthesis of p-galactosidase, permease, and acetylase). 

Add 100 pL of p-galactosidase conjugated secondary antibody diluted in PBS/ FCS. Incubate at room temperature for lh. 

Figure 4. Sorption of p-galactosidase by collagen preparations (samples as in Figure 2) at different degrees of lysine content as a double reciprocal plot for control, Ac — 14 X 10 6 for 15% modification, A0 — 0.53 X 10 6 for 30% modification, Ac = 0.41 X 10 6 for upper curve, A = 0.18 X 10 6 mol/g collagen,...

Another problem that may arise is that the protein fusion may lead to inactivation of the enzyme. The destabilization of P-galactosidase when using a polyphenylalanine lag is an illustradve example (80). There may also be interference between SH groups on the protein and cysteine groups on the fused affinity tail. 

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