A single rainbow trout cobalamin-binding protein stands in for three human binders
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A single rainbow trout cobalamin-binding protein stands in for three human binders. / Greibe, Eva; Fedosov, Sergey; Sorensen, Boe S; Højrup, Peter; Poulsen, Steen Seier; Nexo, Ebba.
I: The Journal of Biological Chemistry, Bind 287, Nr. 40, 28.09.2012, s. 33917-25.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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T1 - A single rainbow trout cobalamin-binding protein stands in for three human binders
AU - Greibe, Eva
AU - Fedosov, Sergey
AU - Sorensen, Boe S
AU - Højrup, Peter
AU - Poulsen, Steen Seier
AU - Nexo, Ebba
PY - 2012/9/28
Y1 - 2012/9/28
N2 - Cobalamin uptake and transport in mammals are mediated by three cobalamin-binding proteins: haptocorrin, intrinsic factor, and transcobalamin. The nature of cobalamin-binding proteins in lower vertebrates remains to be elucidated. The aim of this study was to characterize the cobalamin-binding proteins of the rainbow trout (Oncorhynchus mykiss) and to compare their properties with those of the three human cobalamin-binding proteins. High cobalamin-binding capacity was found in trout stomach (210 pmol/g), roe (400 pmol/g), roe fluid (390 nmol/liter), and plasma (2500 nmol/liter). In all cases, it appeared to be the same protein based on analysis of partial sequences and immunological responses. The trout cobalamin-binding protein was purified from roe fluid, sequenced, and further characterized. Like haptocorrin, the trout cobalamin-binding protein was stable at low pH and had a high binding affinity for the cobalamin analog cobinamide. Like haptocorrin and transcobalamin, the trout cobalamin-binding protein was present in plasma and recognized ligands with altered nucleotide moiety. Like intrinsic factors, the trout cobalamin-binding protein was present in the stomach and resisted degradation by trypsin and chymotrypsin. It also resembled intrinsic factor in the composition of conserved residues in the primary cobalamin-binding site in the C terminus. The trout cobalamin-binding protein was glycosylated and displayed spectral properties comparable with those of haptocorrin and intrinsic factor. In conclusion, only one soluble cobalamin-binding protein was identified in the rainbow trout, a protein that structurally behaves like an intermediate between the three human cobalamin-binding proteins.
AB - Cobalamin uptake and transport in mammals are mediated by three cobalamin-binding proteins: haptocorrin, intrinsic factor, and transcobalamin. The nature of cobalamin-binding proteins in lower vertebrates remains to be elucidated. The aim of this study was to characterize the cobalamin-binding proteins of the rainbow trout (Oncorhynchus mykiss) and to compare their properties with those of the three human cobalamin-binding proteins. High cobalamin-binding capacity was found in trout stomach (210 pmol/g), roe (400 pmol/g), roe fluid (390 nmol/liter), and plasma (2500 nmol/liter). In all cases, it appeared to be the same protein based on analysis of partial sequences and immunological responses. The trout cobalamin-binding protein was purified from roe fluid, sequenced, and further characterized. Like haptocorrin, the trout cobalamin-binding protein was stable at low pH and had a high binding affinity for the cobalamin analog cobinamide. Like haptocorrin and transcobalamin, the trout cobalamin-binding protein was present in plasma and recognized ligands with altered nucleotide moiety. Like intrinsic factors, the trout cobalamin-binding protein was present in the stomach and resisted degradation by trypsin and chymotrypsin. It also resembled intrinsic factor in the composition of conserved residues in the primary cobalamin-binding site in the C terminus. The trout cobalamin-binding protein was glycosylated and displayed spectral properties comparable with those of haptocorrin and intrinsic factor. In conclusion, only one soluble cobalamin-binding protein was identified in the rainbow trout, a protein that structurally behaves like an intermediate between the three human cobalamin-binding proteins.
KW - Amino Acid Sequence
KW - Animals
KW - Concanavalin A
KW - Gene Expression Regulation
KW - Glycosylation
KW - Humans
KW - Hydrogen-Ion Concentration
KW - Intrinsic Factor
KW - Models, Animal
KW - Molecular Sequence Data
KW - Oncorhynchus mykiss
KW - Phylogeny
KW - Protein Binding
KW - Protein Structure, Tertiary
KW - Sequence Homology, Amino Acid
KW - Species Specificity
KW - Transcobalamins
KW - Vitamin B Complex
U2 - 10.1074/jbc.M112.398016
DO - 10.1074/jbc.M112.398016
M3 - Journal article
C2 - 22872637
VL - 287
SP - 33917
EP - 33925
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 40
ER -
ID: 47485995