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Plasma samples are deproteinized by trichloroacetic acid and then the analytes are separated on a μBondapak C18 column (Waters).
Subsequently, proteins were precipitated by trichloroacetic acid and analyzed by SDS-PAGE and immunoblotting.
In both fractionation procedures, proteins were precipitated by trichloroacetic acid and analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and immunoblotting.
CM-P1 and CM-P10 were processed for protein precipitation by trichloroacetic acid, and LC-ESI-MS/MS analyses were carried out on peptides deriving from tryptic digestion of proteins.
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For 2D electrophoresis 150 μg protein of cell lysates were purified by trichloroacetic acid precipitation and re-suspended in DeStreak Rehydration Solution (Amersham Biosciences) containing 0.5% Bio-Lyte pH3-10 (Bio-Rad Laboratories GMünchennchen).
Protein carbonyl formation was measured using a Protein Carbonyl Enzyme Immuno-Assay kit (Biocell Laboratories Inc .. Samples of soluble perlecan treated with peroxynitrite were concentrated by trichloroacetic acid precipitation, and derivatized with 2,4-dinitrophenylhydrazine (DNPH) prior to measurement of protein carbonyls by ELISA as described previously [36].
Apoplastic and whole leaf proteins were precipitated by trichloroacetic acid (TCA)/acetone and purified by phenol-based extraction [ 67, 68].
The ECP fraction was isolated by trichloroacetic acid (TCA) precipitation and the protein pellet was washed thrice with −20°C acetone and then air dried.
Proteins were collected by trichloroacetic acid (TCA) precipitation and analyzed by western blot.
AlmF in assay mixtures was concentrated by trichloroacetic acid (TCA) precipitation and resolved by SDS PAGE.
Cells were lysed with lysis buffer and fragmented double stranded DNA was separated from chromosome-length, unfragmented DNA followed by trichloroacetic acid (TCA) precipitation (Duke and Cohen, 1992).
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