Words similar to submicromolar
Example sentences for: submicromolar
How can you use “submicromolar” in a sentence? Here are some example sentences to help you improve your vocabulary:
The data for both rabbit and yeast Hint enzymes indicate that the dimer's two crystallographically defined nucleotide-binding sites [ 25] bind nucleotide independently and fit well to a single submicromolar K m for each enzyme (Figure 2) [ 30].
2) with a first saturation in the submicromolar range (described below) and a second at much higher concentrations of ThDP.
While compound 14b, containing two phosphorothioylated branches without adenosine, was barely a submicromolar inhibitor, compounds 12b and 13b, which contain respectively three and four CH 2 -phosphorothioadenosyl groups bonded to the central carbon were 40 nM and 65 nM inhibitors.
3in which the uptake at submicromolar concentrations of ThDP is illustrated (open squares).
Human Fhit [ 14 ] and the S. cerevisiae Fhit homolog [ 13 ] , which was called Aph1 but is here termed Hnt2 under nomenclature aproved by the Saccharomyces Genome Database, cleave ApppA more readily while Aph1, the S. pombe homolog, cleaves AppppA more readily [ 20 ] . Consistent with the ApppA hydrolase activity of purified Fhit protein, most cancer cell lines that are Fhit negative at the protein level have higher levels of ApppA than cell lines that are Fhit positive [ 21 ] . Nonetheless, the actual concentrations of dinucleoside polyphosphates were submicromolar in every cell culture sample [ 21 ] and thus, under the reported culture conditions, the measured dinucleoside polyphosphates would not be expected to occupy the Fhit active site substantially [ 19 ] . Dinucleoside polyphosphate levels were measured in adenine-requiring S. cerevisiae strains before or after disruption of the Fhit-homologous HNT2 gene [ 13 ] and in adenine-requiring S. pombe strains as a function of disruption and overexpression of the Fhit-homologous aph1 gene [ 22 ] . Recently, it was observed that diadenosine polyphosphates undergo a divalent cation-dependent conformational change that might mediate their biosynthesis, catabolism or signaling properties [ 23 ] .
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