Expression, receptor binding, and biophysical characterization of guinea pig insulin desB30: a monomeric insulin variant
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Expression, receptor binding, and biophysical characterization of guinea pig insulin desB30 : a monomeric insulin variant. / Engholm, Ebbe; Hansen, Thomas Hesselhøj; Johansson, Eva; Strauss, Holger M.; Vinther, Tine N.; Jensen, Knud Jørgen; Hubálek, Frantisek; Kjeldsen, Thomas B.
I: ChemBioChem, Bind 16, Nr. 6, 2015, s. 954-958.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Expression, receptor binding, and biophysical characterization of guinea pig insulin desB30
T2 - a monomeric insulin variant
AU - Engholm, Ebbe
AU - Hansen, Thomas Hesselhøj
AU - Johansson, Eva
AU - Strauss, Holger M.
AU - Vinther, Tine N.
AU - Jensen, Knud Jørgen
AU - Hubálek, Frantisek
AU - Kjeldsen, Thomas B.
PY - 2015
Y1 - 2015
N2 - Here we report, for the first time, the heterologous expression of desB30 guinea pig insulin (GI desB30) in the yeast Saccharomyces cerevisiae. The affinities of GI desB30 for the insulin receptor A and the IGF-I receptor were also quantified for the first time. Small-angle X-ray scattering and analytical ultracentrifugation studies confirmed that GI desB30 did not form dimers or hexamers, in contrast to human insulin. Sizeexclusion chromatography connected to inductively coupled plasma mass spectrometry revealed that GI desB30 has affinity towards several divalent metal ions. These studies did not indicate the formation of any larger structures of GI desB30 in the presence of various divalent metal ions, but did indicate that GI desB30 has an affinity towards Mn, Co, and Cu ions. Finally, the low affinity for the insulin receptor and the very low affinity for the IGF-I receptor by GI desB30 were quantified.
AB - Here we report, for the first time, the heterologous expression of desB30 guinea pig insulin (GI desB30) in the yeast Saccharomyces cerevisiae. The affinities of GI desB30 for the insulin receptor A and the IGF-I receptor were also quantified for the first time. Small-angle X-ray scattering and analytical ultracentrifugation studies confirmed that GI desB30 did not form dimers or hexamers, in contrast to human insulin. Sizeexclusion chromatography connected to inductively coupled plasma mass spectrometry revealed that GI desB30 has affinity towards several divalent metal ions. These studies did not indicate the formation of any larger structures of GI desB30 in the presence of various divalent metal ions, but did indicate that GI desB30 has an affinity towards Mn, Co, and Cu ions. Finally, the low affinity for the insulin receptor and the very low affinity for the IGF-I receptor by GI desB30 were quantified.
KW - Guinea pig insulin
KW - Insulin expression
KW - Metal affinity
KW - Protein expression
KW - Receptors
U2 - 10.1002/cbic.201402688
DO - 10.1002/cbic.201402688
M3 - Journal article
C2 - 25754940
VL - 16
SP - 954
EP - 958
JO - ChemBioChem
JF - ChemBioChem
SN - 1439-4227
IS - 6
ER -
ID: 135365708