molecular biology - Can I elute my GFP-tagged protein off anti-GFP antibody using a peptide?

I found a paper that describes a method to purify GFP fusion proteins using affinity chromatography: "Purification of GFP fusion proteins with high purity and yield by monoclonal antibody-coupled affinity column chromatography" (1). Unfortunately I don't have access to the full text, so I can't check how exactly they elute the GFP fusion protein from the column. They describe a specific monoclonal antibody they use, there should be information on how to obtain it in the paper.

Abstract:

GFP has often been used as a marker of gene expression, protein
localization in living and fixed tissues as well as for protein
targeting in intact cells and organisms. Monitoring foreign protein
expression via GFP fusion is also very appealing for bioprocess
applications. Many cells, including bacterial, fungal, plant, insect
and mammalian cells, can express recombinant GFP (rGFP) efficiently.
Several methods and procedures have been developed to purify the rGFP
or recombinant proteins fused with GFP tag. However, most current GFP
purification methods are limited by poor yields and low purity. In the
current study, we developed an improved purification method, utilizing
a FMU-GFP.5 monoclonal antibody (mAb) to GFP together with a
mAb-coupled affinity chromatography column. The method resulted in a
sample that was highly pure (more than 97% homogeneity) and had a
sample yield of about 90%. Moreover, the GFP epitope permitted the
isolation of almost all the active recombinant target proteins fused
with GFP, directly and easily, from the crude cellular sources. Our
data suggests this method is more efficient than any currently
available method for purification of GFP protein.

(1) Zhuang R. et al., Purification of GFP fusion proteins with high purity and yield by monoclonal antibody-coupled affinity column chromatography. Protein Expr Purif 2008, 59(1), 138-43