L5263
Lyticase from Arthrobacter luteus
partially purified powder, ≥1,500 units/mg protein
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About This Item
form
partially purified powder
specific activity
≥1,500 units/mg protein
composition
Protein, ≥10% biuret
storage temp.
2-8°C
Biochem/physiol Actions
Lyticase hydrolyzes poly-β(1→3)-glucose such as yeast cell wall glucan.
Physical form
Partially purified powder containing ammonium sulfate and stabilizer
Other Notes
One unit will produce a ΔA800 of 0.001 per min at pH 7.5 at 25 °C, using a suspension of yeast as substrate in a 3 mL reaction mixture.
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
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signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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Related Content
Sanford J Silverman et al.
Proceedings of the National Academy of Sciences of the United States of America, 107(15), 6946-6951 (2010-03-26)
Oscillations in patterns of expression of a large fraction of yeast genes are associated with the "metabolic cycle," usually seen only in prestarved, continuous cultures of yeast. We used FISH of mRNA in individual cells to test the hypothesis that
Markus M M Bisschops et al.
Biochimica et biophysica acta, 1864(1), 231-242 (2016-11-08)
Non-dividing Saccharomyces cerevisiae cultures are highly relevant for fundamental and applied studies. However, cultivation conditions in which non-dividing cells retain substantial metabolic activity are lacking. Unlike stationary-phase (SP) batch cultures, the current experimental paradigm for non-dividing yeast cultures, cultivation under
Sean J Garrity et al.
Proceedings of the National Academy of Sciences of the United States of America, 107(23), 10596-10601 (2010-05-21)
Prions are infectious, self-propagating protein aggregates that have been identified in evolutionarily divergent members of the eukaryotic domain of life. Nevertheless, it is not yet known whether prokaryotes can support the formation of prion aggregates. Here we demonstrate that the