P-D-Galactosidases

DPDPB has been used to study the endocytosis of cadherin from intracellular junctions (Troyanovsky et al., 2006), the subunit arrangement in the flagellar rotor assembly (Lowder et al., 2005), and the disease-associated mutations in myelin proteolipid protein in the endoplasmic reticulum (ER) (Swanton et al., 2005). DPDPB can be used to conjugate reduced antibody molecules to p-D-galactosidase using essentially the same protocol as that described by O Sullivan et al. (1979). 

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... 

C. T. Yuen, R. G. Price, L. Chattagoon, A. C. Richardson, and P. F. G. Praill, Colorimetric assays for /V-acetyl-P-D-glucosaminidase and P-D-galactosidase in human urine using newly developed ra-nitros-tyryl substrates, Clin. Chem. Acta, 124 (1981) 195-204. 

I. Pocsi, S. A. Taylor, A. C. Richardson, B. V. Smith, and R. G. Price, Comparison of several new chromogenic galactosides as substrates for various p-D-galactosidases, Biochim. Biophys. Acta, 1163 (1993) 54-60. 

D. E. Walker and B. Axelrod, Evidence for a single catalytic site on the P-d-glucosidase-P-D-galactosidase of almond emulsin, Arch. Biochem. Biophys., 187 (1978) 102-107. 

K. Bock and K. Adelhorst, Derivatives of methyl p-lactoside as substrates for and inhibitors of p-D-galactosidase fromil. coli, Carbohydr. Res., 202 (1990) 131-149. 

M. Yde and C. K. De Bruyne, Binding of substituted phenyl 1-thio-P-D-galactopyranosides to P-D-galactosidase from E. coli, Carbohydr. Res., 60 (1978) 155-165. 

Fujiwara, K., Matsumoto, N., Yagisawa, S., Tanimori, H., Kitagawa, T., Hirota, M., Hiratani, K., Fukushima, K., Tomonaga, A., Hara, K., and Yamamoto, K. (1988) Sandwich enzyme immunoassay of tumor-associated antigen sialosylated Lewis31 using p-D-galactosidase coupled to a monoclonal antibody of IgM isotype. J. Immunol. Methods 112, 77—83. 

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. 

Kato, K., Hamaguchi, Y., Fukui, H., and Ishikawa, E. (1975b) Enzyme-linked immunoassay. II. A simple method for synthesis of the rabbit antibody-p-D-galactosidase complex and its general applicability./. Biochem. (Tokyo) 78, 423. 

Mori and Okahata (1998) Batch Transgalactosylation from 1-O-p-nitrophenyl-P- D-galactopyranoside to 5-phenylpentan-l-ol P- D-galactosidase... 

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. 

Chemiluminescence immunoassay methods have many applications (Weeks, 1992). Highly sensitive chemiluminescent immunoassays were developed by Tsuji et al. (1989) for determination of enzymes (oxidases, peroxidase, glucose oxidase, P-D-galactosidase) as well as various hormones and drugs in biological fluids (Tsuji et al., 1989). 

The enzymes most frequently used for protein labeling are horse radish peroxidase, alkaline phosphatase, glucose oxidase, glucoamylase, p-D-galactosidase, lysosym. 

Immobilized metal-affinity chromatography Na+-dependent alanine-insensitive proline uptake system (SLC6A20) Integrin-mobilferrin pathway membrane protein system involved in the transport of ferric iron also inosine-5 - monophosphate Inducible oxide synthetase Iifitiator element Inositol 1,4,5-triphosphate Immobilized pH gradient Isopropylthio-p-D-galactosidase Isopropylthio-p-D-galactopyranoside Inverted repeat insulin receptor... 

Yuen CT> Price RG, Chattagoon L, Richardson AC, Praill PPG. Colorimetric assays for N-acetyl-(3-D-glucosaminidase and p-D galactosidase in human urine using newly developed v-nitrostyryl substrates. Clin Chim Acta 1982 124 195-204. 

The 1,2-dioxetanes have mainly been used to develop substrates for the determination of enzymes, the more significant examples being (3-(2 -spiroada-mantane)-4-methoxy-4-(3"-phosphoryloxy) phenyl-1,2-dioxetane sodium salt (AMPPD), a substrate for alkaline phosphatase, and its galactopyranosyl derivative, (3-(2 -spiroadamantane)-4-methoxy-4-(3"-p-D-galactopyranosyloxyphcnyl )-1,2-dioxetane sodium salt (AMPGD), a substrate for p-D-galactosidase. 

With the interest in glycosidase inhibitors, compounds lending insight to the structures and mechanisms of these enzymes have received much attention. Recently, Lehmann, et al.,27 prepared a series of diastereotopic C-glycosides designed to be substrates for p-D-galactosidase. The premise was that in order to confirm this enzyme s mechanism of action, proposed from an extrapolation of lysozyme activity,28 31 the structural analysis of products resulting from the enzyme s effect on its substrates would be helpful. Therefore, the structures... 

Using an a-L-fficosidase from beef kidney, it was possible to remove approximately 85% of the fucose from the xyloglucan from runner bean cell wall (O Neill and Selvendran, 1983). However, attempts to hydrolyse terminal galactose residues with either a or p-galactosidases were unsuccessful. Kato and Matsuda (1980a,b) found that the exo-P-D-galactosidase... 

DPDPB can be used to conjugate reduced antibody molecules to p-D-galactosidase using essentially the same protocol as that described by O Sullivan et al. (1979). 

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