ArticleAnalytical biochemistry2010
A long-wavelength fluorescent substrate for continuous fluorometric determination of alpha-mannosidase activity: resorufin alpha-D-mannopyranoside.
Article in Analytical biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 14 citations in OpenAlex.
- Miniaturization of a colorimetric cellulase activity assay on a microfluidic sensor platform.RSC advances · 2025Article
- Benzylic Trifluoromethyl Accelerates 1,6-Elimination Toward Rapid Probe Activation.bioRxiv : the preprint server for biology · 2024Article
- Identification of a potential allosteric site of Golgi α-mannosidase II using computer-aided drug design.PloS one · 2019Article
- Rotamer-Restricted Fluorogenicity of the Bis-Arsenical ReAsH.Journal of the American Chemical Society · 2016Article
- Probing the target-specific inhibition of sensitized protein tyrosine phosphatases with biarsenical probes.Organic & biomolecular chemistry · 2015Article
- High throughput nanostructure-initiator mass spectrometry screening of microbial growth conditions for maximal β-glucosidase production.Frontiers in microbiology · 2013Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
A simple and reliable continuous assay for measurement of alpha-mannosidase activity is described and demonstrated for analysis with two recombinant human enzymes using the new substrate resorufin alpha-d-mannopyranoside (Res-Man). The product of enzyme reaction, resorufin, exhibits fluorescence emission at 585 nm with excitation at 571 nm and has a pK(a) of 5.8, allowing continuous measurement of fluorescence turnover at or near physiological pH values for human lysosomal and Drosophila Golgi alpha-mannosidases. The assay performed using recombinant Drosophila Golgi alpha-mannosidase (dGMII) has been shown to give the kinetic parameters K(m) of 200 microM and V(max) of 11 nmol/min per nmol dGMII. Methods for performing the assay using several concentrations of the known alpha-mannosidase inhibitor swainsonine are also presented, demonstrating a potential for use of the assay as a simple method for high-throughput screening of inhibitors potentially useful in cancer treatment.
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Registered trials
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