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3rd attempt in vitro assay of WelO16 with h. welwtischii lysate lyophilized assay sample and solved in MeOH
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2025-02-04
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Barber et al Nature Protocols Source Data - Figure 4.xlsx
Figure 4: Data for representative chromatograms showing efficient separation of the expected substrates and products of maltooligosaccharides in the α-amylase assay and low molecular
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Extracellular enzyme activities of strains from clades 1–4 grown at different NaCl concentrations at 24°C.
+, all tested strains showed measurable enzyme activity;–, no tested strain showed measurable enzyme activity; +/–, 50% or more tested strains showed measurable enzyme activity;–/+, 50% or less showed
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Dead-end inhibition patterns and inhibition constants for oxalate and AMP in TpPK.
Inhibition patterns were taken from the double reciprocal plots of the inhibition experiments (Fig. 3). Simple inhibition patterns were confirmed from linear replots of the slopes or intercepts versus
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Enzymatic efficiencies determinations for selected subset of strains representative of each mutation type.
aCovalent FAD is expressed in pmol covalend FAD mg of protein−1 and is an estimation of the total amount of succinate dehydrogenase enzyme present in the mitochondrial preparation, presented values ar
NIAID Data Ecosystem40
Effects of activators on phosphotransferase activity in crude extracts of Y and N strains.
Activity is expressed as mU/mg. N represents the strain expressing cN-II whereas Y the control strain. Assay was performed as described in Experimental Procedures. Values are the mean±SD of at least t
Figshare2015-12-02 更新30
