The complex velocity of the attenuated wave in the medium is resolved to calculate its propagation (phase) velocity and quality factor of attenuation.
The complex slowness vector of the attenuated wave in the medium is resolved to calculate its propagation (phase) velocity, quality factor and angle of attenuation.
Two NGG inconsistencies under the minimal medium and one under the YP medium were resolved by relaxing the irreversibility of at least two reactions.
Aliquots of lyophilized human MNC-secretome and control medium were resolved in the different basal media at a 10-fold concentration (lyophilized secretome, derived from 25×10 cells/mL).
Samples of cytosolic protein (10 μg), prepared by centrifugation of the homogenate at 4500 r.p.m. for 10 min, or neat tissue culture medium, were resolved on 12% SDS PAGE.
To detect the secretion levels of wild-type Wnt3a and mutant isoforms, equal amounts of conditioned medium were resolved on 12% SDS-PAGE and analyzed by Western blot using anti-Wnt3a antibody.
A 1-ml aliquot of the 20× concentrated cell medium with nascent HDL was resolved into 1-ml fractions on a calibrated HiLoad 16/60 Superdex 200 gel-filtration column (GE Healthcare, Mickleton, NJ, USA).
The same amount of medium protein (8.7 μg/lane) was resolved on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE, 7.5% acrylamide gel) containing 0.1% gelatin under nonreducing conditions.
The medium was removed, and the dye was resolved with 100 μL of isopropanol (Hedinger GmbH & Co. KG, Stuttgart, Germany).
For zymography, the protein extracts from the pellets, the ammonium sulfate (80%%) concentrated proteins from the medium, or ÄKTA-purified α-amylase was resolved in native 10%% PAA gel, supplemented with 1 % of liquefied soluble starch, and added prior to polymerization.
