Re: puzzling protein

Deb McMillen (mcmillen@morel.uoregon.edu)
Thu, 13 May 1999 17:39:29 -0700 (PDT)

Lanie, I can't answer all of your questions, but yes, Coomassie blue
comes out in its own broad peak on RP HPLC--it is only electrostatically
associated with the proteins and in TFA/acetonitrile migrates according to
its own hydrophobicity. You might be lucky (or unlucky) enough to have a
protein co-migrating with the CB.
About the IgG--5 micron C18 Reverse Phase columns generally won't let
large proteins through--I think the upper limit is about 100,000
daltons--may be smaller depending on the protein. So if you are looking
for something large it is stuck on the column--and some proteins stick on
the frit, never entering the column.

Hope this small piece is helpful,
Deb McMillen
Institute of Molecular Biology
University of Oregon
Eugene OR 97403

On Thu, 13 May 1999, Helene Z. Hill, Ph.D. wrote:

> I hope that one of you out there can figure this one out. Here are the facts:
> 1. Serum-free conditioned medium from cultured melanoma cells rescues irradiated and chemotherapy-treated cells from death (colony-forming ability). It was concentrated and separated by preparative zonal electrophoresis (PZE).
> 2. Neutralizing antiserum (As50) was obtained using activity fractions from PZE. On western, the antiserum reacts with 2 proteins of about 40 kD in the fractions that have activity in the bioassay. I call the 2 proteins upper and lower.
> 3. On MALDI-MS, lower could not be identified and upper appeared to be actin but we now know it is contaminated with actin.
> 4. Upper and lower were excised from coomassie-stained prep gels, electroeluted, concentrated and treated with BioBeads to get rid of remaining SDS and added PBS (no Ca or Mg). Added anti-Actin (Sigma) at 1/400 to upper and incubated at 4 deg over the weekend. Centrifuged 30 min in microfuge. SDS-PAGE and western showed that pptn was incomplete. Upper SN contains upper protein, actin and actin-antibody complex. Upper SN, lower and Sigma actin were run on HPLC in 0.1% THF and acetonitrile 0-60% at 1 ml/min. Actin elutes at 7-8 minutes. There were 3 bands for upper SN, 5-7, 43-44 and 64-66 minutes. The last was intensely blue. There were 3 bands for lower, 2 at 5-7 min which I pooled and one at 61-63 min which was intensely blue. We assumed that the proteins we were purifying would be where the blue was. The peak samples were concentrated by speed-vac, resuspended in 0.0625M tris pH 6.8 and 20% of each (10% of the blue fractions since these were the biggest peaks) wa!
s run on SDS-PAGE for westerns along with actin. Actin ran at about 40 kD and was the only lane that reacted with actin Ab. Upper fractions 5-7 and 43-44 had strong reactions with As50 but the MW of both was ~57 kD (remember it started at ~40!). Lower fractions 5-7 ran funny but was slaunchwise between 40 and 57 kD, a repeat ran at 57 kD. The blue fractions did not react with either antibody.
> 5. So where did the actin go in the HPLC?
> How come proteins that were about 40 kD became 57 kD after HPLC?
> Why do the fractions that contain the coomassie stain appear to be empty of protein?
> Did the HPLC reagents strip the dye from the proteins?
> Can anyone tell me a better way to get the actin out of upper?
> Does anyone know where to expect the immunoglobin or the complex to come off in the HPLC?
>
> You all have been wonderfully helpful before. I have learned a lot from your e-mail conversations with each other. I am learning all of this the hard way and these latest results really have me baffled. Any help I can get would be greatly appreciated.
>
> Lanie Hill
>
> Helene Z. Hill, Ph.D.
> Professor of Radiology
> NJ Medical School
> Newark, NJ 07103-2714
> Tel:973-972-3421
> Fax:973-972-5592
>
>