Journal Article10.1016/J.BIOS.2013.05.005
A novel thermometric biosensor for fast surveillance of β-lactamase activity in milk
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TL;DR: A fast, sensitive and convenient method based on enzyme thermistor (ET) for the surveillance of β-lactamase in milk with the advantages of high throughput, timesaving and accurate quantification made this method an ideal alternative for routine use.
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About: This article is published in Biosensors and Bioelectronics. The article was published on 15 Nov 2013.
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Citations
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Methods in Enzymology.
TL;DR: This volume is keyed to high resolution electron microscopy, which is a sophisticated form of structural analysis, but really morphology in a modern guise, the physical and mechanical background of the instrument and its ancillary tools are simply and well presented.
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Sensitive and selective near-infrared fluorescent off-on probe and its application to imaging different levels of β-lactamase in Staphylococcus aureus.
TL;DR: The validity of the probe has been confirmed by determining β-lactamase in human urine samples in comparison with that determined by iodimetry, and by taking advantage of its high sensitivity and NIR emission feature, it has been utilized to image β- lactamases in three types of Staphylococcus aureus.
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Translating molecular detections into a simple temperature test using a target-responsive smart thermometer.
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References
•Journal Article
Methods in Enzymology.
TL;DR: This volume is keyed to high resolution electron microscopy, which is a sophisticated form of structural analysis, but really morphology in a modern guise, the physical and mechanical background of the instrument and its ancillary tools are simply and well presented.
3.6K
Updated Functional Classification of β-Lactamases
Karen Bush,George A. Jacoby +1 more
TL;DR: The functional classification scheme updated herein is based on the 1995 proposal and includes group 1 (class C) cephalosporinases; group 2 (classes A and D) broad-spectrum, inhibitor-resistant, and extended-spectrums β-lactamases and serine carbapenemases; and group 3 metallo-β-lacticamases.
2.2K
An Enzyme from Bacteria able to Destroy Penicillin
Edward P. Abraham,E. Chain +1 more
TL;DR: It is confirmed that the growth of B. coli and a number of other bacteria belonging to the colityphoid group was not inhibited by penicillin, and the cause of the resistance of these organisms to the action of Penicillin is found.
1.4K
Enzymatic hydrogelation of small molecules.
Zhimou Yang,Gaolin Liang,Bing Xu +2 more
TL;DR: In this Account, the design and application of enzyme-catalyzed or -regulated formation of supramolecular hydrogels that offer a new strategy for detecting the activity of enzymes, screening for enzyme inhibitors, typing bacteria, drug delivery systems, and controlling the fate of cells are illustrated.
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