Relevant bibliographies by topics / 4-methylumbelliferyl substrates

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Academic literature on the topic '4-methylumbelliferyl substrates'

Author: Grafiati
Published: 3 June 2025
Last updated: 31 July 2025

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Journal articles on the topic "4-methylumbelliferyl substrates"

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Garcia-Sastre, A., E. Villar, J. C. Manuguerra, C. Hannoun, and J. A. Cabezas. "Activity of influenza C virus O-acetylesterase with O-acetyl-containing compounds." Biochemical Journal 273, no. 2 (1991): 435–41. http://dx.doi.org/10.1042/bj2730435.

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Influenza C virus (strain C/Johannesburg/1/66) was grown, harvested, purified and used as source for the enzyme O-acetylesterase (N-acyl-O-acetylneuraminate O-acetylhydrolase; EC 3.1.1.53). This activity was studied and characterized with regard to some new substrates. The pH optimum of the enzyme is around 7.6, its stability at different pH values shows a result similar to that of the pH optimum, and its activity is well maintained in the pH range from 7.0 to 8.5 (all these tests were performed with 4-nitrophenyl acetate as substrate). Remarkable differences were found in the values of both K
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2

Bhat, K. M., A. J. Hay, M. Claeyssens та T. M. Wood. "Study of the mode of action and site-specificity of the endo-(1→4)-β-d-glucanases of the fungus Penicillium pinophilum with normal, 1-3H-labelled, reduced and chromogenic cello-oligosaccharides". Biochemical Journal 266, № 2 (1990): 371–78. http://dx.doi.org/10.1042/bj2660371.

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The modes of action of the five major endo-(1→4)-beta-D-glucanases (I, II, III, IV and V) purified from Penicillium pinophilum cellulase were compared by h.p.l.c. analysis, with normal, 1-3H-labelled and reduced cello-oligosaccharides and 4-methylumbelliferyl glycosides as substrates. Significant differences were observed in the preferred site of cleavage even when substrates with the same number of glycosidic bonds were compared. Thus, although endoglucanase I was unable to attack normal cello-oligosaccharides shorter than degree of polymerization 6, it hydrolysed reduced cellopentaose to yie
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3

Barth, M. G. M., and P. D. Bridge. "4-Methylumbelliferyl substituted compounds as fluorogenic substrates for fungal extracellular enzymes." Letters in Applied Microbiology 9, no. 5 (1989): 177–79. http://dx.doi.org/10.1111/j.1472-765x.1989.tb00318.x.

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4

Miller, Morten, Ansa Palojärvi, Andrea Rangger, Morten Reeslev, and Annelise Kjøller. "The Use of Fluorogenic Substrates To Measure Fungal Presence and Activity in Soil." Applied and Environmental Microbiology 64, no. 2 (1998): 613–17. http://dx.doi.org/10.1128/aem.64.2.613-617.1998.

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ABSTRACT Our objective was to determine if 4-methylumbelliferyl-labelled enzyme substrates could be used to detect and quantify specific components of chitinase and cellulase activities as specific indicators of the presence and activity of fungal biomass. The fluorogenic substrates 4-methylumbelliferyl (MUF)N-acetyl-β-d-glucosaminide and MUF β-d-lactoside were used for the detection and quantification of β-N-acetylglucosaminidase (EC 3.2.1.30 ) (NAGase) and endo 1,4-β-glucanase (EC 3.2.1.4 )/cellobiohydrolase (EC3.2.1.91 ) (CELase), respectively. Culture screenings on solid media showed a wid
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5

Adcock, Philip W., and Christopher P. Saint. "Rapid Confirmation of Clostridium perfringens by Using Chromogenic and Fluorogenic Substrates." Applied and Environmental Microbiology 67, no. 9 (2001): 4382–84. http://dx.doi.org/10.1128/aem.67.9.4382-4384.2001.

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ABSTRACT The use of 4-methylumbelliferyl phosphate (MUP) andortho-nitrophenyl-β-d-galactopyranoside (ONPG) for the identification of Clostridium perfringenswas investigated. A liquid assay containing both MUP and ONPG was a highly specific alternative method for C. perfringensconfirmation, reducing incubation time from 48 to only 4 h. The assay solution is easy to prepare, does not require anaerobic conditions for use, and has an extended shelf life.
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Fiksdal, L., I. Tryland, and H. Nelis. "Rapid detection of coliform bacteria and influence of non-target bacteria." Water Science and Technology 35, no. 11-12 (1997): 415–18. http://dx.doi.org/10.2166/wst.1997.0769.

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Enzymatic hydrolysis of fluorogenic substrates (4-methylumbelliferyl-β-D-galactoside, 4-methylumbelliferyl-β-D-glucuronide) has been used for rapid (25min) detection of indicators of faecal water pollution, i.e. coliform and thermotolerant coliform bacteria. In the present work, enzymatic activities and different groups of bacteria (i.e. thermotolerant coliforms, coliforms, β-galactosidase positive and β-glucuronidase positive bacteria) from sewage effluent and polluted river water have been investigated. Ratios of the order of 1:10 between coliforms and β-galactosidase positive bacteria were
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7

Bussink, Anton P., Marri Verhoek, Jocelyne Vreede, et al. "Common G102S polymorphism in chitotriosidase differentially affects activity towards 4-methylumbelliferyl substrates." FEBS Journal 276, no. 19 (2009): 5678–88. http://dx.doi.org/10.1111/j.1742-4658.2009.07259.x.

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8

Luyten, G. P., A. T. Hoogeveen, and H. Galjaard. "A fluorescence staining method for the demonstration and measurement of lysosomal enzyme activities in single cells." Journal of Histochemistry & Cytochemistry 33, no. 9 (1985): 965–68. http://dx.doi.org/10.1177/33.9.3926869.

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A cytochemical fluorescence method is described that makes possible simple, rapid, and specific demonstration and measurement of the activities of a wide variety of lysosomal enzymes in single cells using 4-methylumbelliferyl derivatives as substrates. The validity of the method and a number of applications using normal and mutant human cells are presented.
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Thompson, Hayley, Karen A. Homer, Susmitha Rao, Veronica Booth, and Arthur H. F. Hosie. "An Orthologue of Bacteroides fragilis NanH Is the Principal Sialidase in Tannerella forsythia." Journal of Bacteriology 191, no. 11 (2009): 3623–28. http://dx.doi.org/10.1128/jb.01618-08.

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ABSTRACT Sialidase activity is a putative virulence factor of the anaerobic periodontal pathogen Tannerella forsythia, but it is uncertain which genes encode this activity. Characterization of a putative sialidase, SiaHI, by others, indicated that this protein alone may not be responsible for all of the sialidase activity. We describe a second sialidase in T. forsythia (TF0035), an orthologue of Bacteroides fragilis NanH, and its expression in Escherichia coli. Sialidase activity of the expressed NanH was confirmed by using 2′-(4-methylumbelliferyl)-α-d-N-acetylneuraminic acid as a substrate.
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10

Kämpfer, Peter, Richard Keuch, and Wolfgang Dott. "Glycosidase profiles of Bacillus spp. and their value for species differentiation." Canadian Journal of Microbiology 39, no. 8 (1993): 808–11. http://dx.doi.org/10.1139/m93-119.

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A total of 268 strains of Bacillus spp. were investigated for their ability to hydrolyze 14 different fluorogenic 4-methylumbelliferyl-linked glycosidase substrates within 6 and 24 h of incubation. Glycosidase profiles were heterogeneous within the genus and some of the tests showed high separation index values; the profiles can therefore improve the differentiation of Bacillus spp. However, glycosidase profiles are not sufficient for unambiguous identification and should be used in combination with other biochemical tests.Key words: Bacillus, glycosidases, fluorogenic substrates, differentiat
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Conference papers on the topic "4-methylumbelliferyl substrates"

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Gunda, Naga Siva Kumar, Selvaraj Naicker, Maryam S. Ghoraishi, Subir Bhattacharjee, Thomas G. Thundat, and Sushanta K. Mitra. "Microspot With Integrated Wells (MSIW) for the Detection of E.coli." In ASME 2013 11th International Conference on Nanochannels, Microchannels, and Minichannels. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/icnmm2013-73037.

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There is an increasing problem in getting quality water for developing countries. Water system is contaminated and without proper treatment, it has been consumed as drinking water. It is a big problem for health. Escherichia coli (E.coli) is the main cause for the contamination of water and illness in people. Early detection of E.coli presence in the drinking water followed by subsequent treatment for elimination of E.coli can solve this problem. The present work developed a new method for detecting E.coli in contaminated water using microspot with integrated wells (MSIW). The method involves
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