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1  region, corresponding to approximately 0.04 zmol (24 molecules) per reaction.
2  +/- 0.2 zmol pg(-1) s(-1) and 0.04 +/- 0.08 zmol pg(-1) s(-1), respectively, for single LNCaP cells
3  epitope peptide was degraded at 8.9 +/- 0.1 zmol muM(-1) s(-1), but with differential fragment forma
4  similar to one another (0.02, 0.06, and 0.1 zmol pg(-1) s(-1), for PANC-1, CFPAC-1, and HPAF-II cell
5                      Detection limits were 1 zmol for BODIPY-FL and 500 ymol for tetramethylrhodamine
6 biting a detection limit of approximately 10 zmol (approximately 6000 molecules) for smaller proteins
7 as determined as ca. 20 pM (equivalent to 10 zmol) of a cyanine fluorophore, Cy5.
8  the assay for biotin was 1 x 10(-15) M (100 zmol of biotin in the sample).
9 proximately 7000 molecules (approximately 11 zmol) at individual electrodes are reported, allowing pr
10 es containing 300 zmol of maltopentaose, 132 zmol of alpha-cyclodextrin, and 14 zmol (approximately 8
11 aose, 132 zmol of alpha-cyclodextrin, and 14 zmol (approximately 8400 molecules) of gramicidin S are
12                          The detection of 14 zmol of gramicidin S is to the best of our knowledge a r
13 5 fM and mass detection limits of 150 +/- 15 zmol for Chromeo P540 labeled beta-lactoglobulin.
14 ount released per event ranged from 8 to 170 zmol.
15 d phosphorylation was on average 0.1 +/- 0.2 zmol pg(-1) s(-1) and 0.04 +/- 0.08 zmol pg(-1) s(-1), r
16 tentagged probe with a detection limit of 25 zmol (2.5 x 10(-20) mol).
17 s offer a greatly lower detection limit (250 zmol), as compared to common bioassays' spherical nanopa
18 fM and mass detection limits were 310 +/- 30 zmol with pH 4-8 ampholytes.
19 rovide a detection limit of approximately 30 zmol (approximately 18,000 molecules) for proteins with
20 s in a given fraction varied from 0 to 1,300 zmol.
21 this configuration is demonstrated to be 300 zmol for the phosphopeptide RRREEE(pS)EEEAA using multis
22 gnals obtained from particles containing 300 zmol of maltopentaose, 132 zmol of alpha-cyclodextrin, a
23  3, signal/RMS noise) ranged from 100 to 300 zmol, for the six Ang-I variants.
24 M, which corresponds to the injection of 335 zmol of peptide.
25 -CEM cells are 11.1 +/- 0.5 and 10.6 +/- 0.4 zmol, respectively.
26 n 2.1-micron-i.d. capillaries range from 4.4 zmol (approximately 2700 molecules) for aflatoxin B2 to
27 by a limit of detection of approximately 400 zmol, while providing a mass measurement accuracy of 1 p
28 es and demonstrated a detection limit of 400 zmol for fluorescein.
29  < 10(-8) M for amino acids and 10(-9)M (425 zmol) for fluorescein.
30 scribed with detection limits of 320 pM (430 zmol).
31  The 40 min assay has a detection limit of 5 zmol ( approximately 3 000 molecules) of CIP.
32 lting in a lower limit of quantitation of 50 zmol (14)C/peak.
33 erage quantity determined at one cell was 52 zmol.
34  (129 pg) for PAPR and 56 fM (9 pg/mL) or 56 zmol (9 fg) for IgG.
35 oxidase molecules (representing 9.6 fg or 60 zmol of protein), about 10(6) times fewer than classical
36 The developed reader offers the unmatched 60 zmol detection limit and 7-order linear dynamic range fo
37  detection limits as low as approximately 70 zmol (approximately 42,000 molecules).
38 s were enabled by ultrahigh sensitivity (<75 zmol for individual proteins) achieved using high-effici
39  Abl kinase sensor fragmented at 4.2 +/- 4.8 zmol muM(-1) s(-1) and the majority of cells possessed s
40 liminary mass detection limit of 0.7 ag or 8 zmol are determined for rubidium using a compact laser d
41 ound to be 10 fg/mL which is equivalent to 8 zmol in the 70-microL sample.
42 amounts of analytes (e.g., approximately 800 zmol of verapamil) with a dynamic range spanning up to 4
43 hile the LOD for 32P-labeled analytes is 4.9 zmol (0.33 pM or 0.002 Bq), with a linear range for 35S-

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