i need to understand on how to neutralize the tca in supernatant after protein precipitation. I am interested in the deproteinized part and not the pellet proteins. Can an equal volume of Tris pH 8.8 do the job? or more is required
Why you are preferring the TCA precipitation if your analytes of interest are being affected by an acidic environment? Salt induced (salting out) precipitation or acetone/ACN precipitation can also do the job if your sample matrix is convenient. There are also other traditional methods available such as depletion/protein removal plates.
By the way, related the asking question about using tris at pH 8.8 may work for neutralization but the most accurate results can be obtained by experimental approach since added volume and molarity should be in consideration due to get appropriate stochiometry.