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. Author manuscript; available in PMC: 2010 Aug 1.
Published in final edited form as: Protein Expr Purif. 2009 Feb 21;66(2):121–130. doi: 10.1016/j.pep.2009.02.012

Table 1.

Structural Changes in the Sequence of Residues 41-52 of Human Prolactin.

Structural Change
Yield
Agonist Activity
Protein Residues 35-55 with deletions or replacements underlined Monomer yield Monomer percentage ED50 (nM) Fold decrease
WT hPRL EMFSEFDKRYTHGRGFITKAI 15.4 mg 90% 0.23 1
Δ41-52 hPRL EMFSEFKAI 9.4 mg 42% 702.42 3041
G2-ΔhPRL EMFSEFGGKAI 2.7 mg 39% 5.25 23
G3-ΔhPRL EMFSEFGGGKAI 7.9 mg 40% 18.91 82
G4-ΔhPRL EMFSEFGGGGKAI 13.5 mg 57% 1277.16 5312
G5-ΔhPRL EMFSEFGGGGGKAI 11.4 mg 67% 1.36 6
A2-ΔhPRL EMFSEFAAKAI 6.2 mg 34% 163.38 707
SPGG-ΔhPRL EMFSEFSPGGKAI 8.7 mg 49% 0.44 2
DGFIT-ΔhPRL EMFSEFDGFITKAI 17.5 mg 52% 45.94 207
DIT-ΔhPRL EMFSEFDITKAI 13.4 mg 70% 47.93 199
G129R hPRL ------- 18.3 mg 90% 5.99 26