The figures illustrate that the absence
of salt affects the chromatography of
globular proteins, slightly delaying peak
elution and broadening the peaks giving
less definition between monomers and
higher oligomers. This is consistent for
all three proteins. The higher molecular
weight species seen in the presence
of salt are not visible in the traces in
which the mobile phase did not contain
NaCl, presumably due to retention and
there is a shift in the protein elution
time in the absence of salt indicating
that the protein is being partially
retained on the column. This suggests
that the presence of salt reduces the
interaction of protein with the matrix.