High strength extracts on the other hand can show "a more precipitous, and more terrifying, face" and many who try it this way may never wish to repeat the experience.
We were not able to make comparable measurements of light chain nitrosylation since the high ionic strength extracts had an abundance of low molecular weight proteins that could lead to misidentification of the light chain bands.
High-ionic strength extracts of these muscles were left untreated (endogenous), treated with ascorbate (control), or treated with 10 µM SNO-L-cys (L) and subjected to the coumarin switch assay followed by coomassie staining and protein mass normalization as described earlier.
In addition to total muscle extracts, low-ionic strength extracts were investigated to remove high abundance myofibrillar proteins and improve the detection of low abundance proteins.
The time-dependent interfacial strength is extracted from the results of transverse tensile tests with various loading rates and their fractography in the unidirectional composite.
Then, a distribution of source strength is extracted along the circumference of the rotor at the blade tip radius in each analysed third-octave band.
The physiochemical properties relating to the binding strength were extracted as descriptors by DS 2.5.
Information on the efficacy of bonding is often sought from measurements of bond strength on extracted teeth.
Because myofibrillar proteins may hamper the detection of low abundance proteins, we also precipitated myofibrils at low ionic strength [ 24, 25], and focused on the soluble low ionic strength (LIS) extract.
