Exactly. Without a picture of SEC profile it's even difficult to decipher the 
meaning of "extremely asymmetric peak shape".
Beside that, one domain or multi-domain protein, extended N-term or C-term 
loops containing constructs, column, load (weight & vol) and flow rate - any 
one of these could affect separation efficiency and/or peak characteristics.
Regards,Reza

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____________________________
Md Rezaul Karim, Ph.D.
Postdoctoral Research Fellow
Department of Drug Discovery
H. Lee Moffitt Cancer Center and Research Institute
Tampa, FL 33612
Email: reza.ka...@moffitt.org, rez...@usf.edu
Phone: (813) 745 4673 ext. 5462
https://orcid.org/0000-0002-0424-127X 
 
  On Wed, Dec 9, 2020 at 11:42 AM, Artem Evdokimov<artem.evdoki...@gmail.com> 
wrote:   Probably a good idea to share an image :) worth many words...
Artem
On Wed, Dec 9, 2020, 9:17 AM <MJ Xie> <sz20203020...@cau.edu.cn> wrote:

Dear All
        There is a 43kd protein purified via Ni-chelating affinity 
chromatography, anion exchange chromatography and gel filtration chromatography 
in sequence. However the chromatogram obtained showed an extremely asymmetric 
peak shape. The aggregation forms of proteins are mainly in the range of 
monomers and dimers(Hepes and low concentration of salt were used as buffers 
for gel filtration chromatography). 5% glycerinum and 1mM Benzamidine 
hydrochloride had been added in order to maintain the stability of the protein 
and prevent it from degrading. But well, all the efforts seem to be useless. We 
wonder if there are any effective measures can be taken to radically solve this 
problem. We would be much indebted for the suggestions you offer.


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