The Experts below are selected from a list of 60 Experts worldwide ranked by ideXlab platform
Fares Namour - One of the best experts on this subject based on the ideXlab platform.
-
cubilin and the hydrophobic Intrinsic Factor receptor are distinct molecules
Blood, 2001Co-Authors: Celine Chery, Fares NamourAbstract:Cubilin is a 460-kd multiligand hydrophobic protein that binds to Intrinsic Factor cobalamin (Cbl-IF) with a high affinity and that is expressed in both kidney and ileal epithelial cells. Based on this observation, it has been speculated that cubilin and Intrinsic Factor cobalamin receptor (IFCR)
Jean-pierre Nicolas - One of the best experts on this subject based on the ideXlab platform.
-
Binding assay and physicochemical characteristics of solubilized Intrinsic Factor receptor in ileal mucosal homogenates using phenyl-Sepharose to separate the saturated receptor from free Intrinsic Factor
Biochimica et biophysica acta, 1991Co-Authors: Jean-louis Guéant, H. Schohn, Ralph Gräsbeck, H. Brulé, Monique Saunier, Jean-pierre NicolasAbstract:A radioisotopic assay was set to determine the physicochemical properties of the solubilized Intrinsic Factor receptor in pig mucosal extracts. In this assay, phenyl-Sepharose was used to separate the receptor-Intrinsic Factor-labelled cobalamin complex from the free saturated Intrinsic Factor. The association constant (at pH 7.4) of the receptor-Intrinsic Factor complex was estimated at 3.4 +/- 0.3 nM-1. Adsorption of the apo-receptor to phenyl-Sepharose allowed its binding site to be made accessible to Intrinsic Factor with an association constant in order of 6 nM-1. The receptor binding activity obtained with five mucosal extracts was closely correlated with that obtained by gel filtration of the Intrinsic Factor-receptor complex (r = 0.99). The radioisotope assay was used to detect the unsaturated receptor (apo-receptor) in sucrose density ultracentrifugation and in superose 6 gel filtration. The sedimentation coefficient was 9.5 s. The apo-receptor was eluted in three peaks in gel filtration, corresponding to the formation of oligomers. The peak of the monomer was increased in presence of EDTA. Its molecular mass was estimated at 270 kDa and its Stokes radius at 5.9 nm. It was concluded that calcium is involved in the oligomerisation of the apo-receptor.
Celine Chery - One of the best experts on this subject based on the ideXlab platform.
-
cubilin and the hydrophobic Intrinsic Factor receptor are distinct molecules
Blood, 2001Co-Authors: Celine Chery, Fares NamourAbstract:Cubilin is a 460-kd multiligand hydrophobic protein that binds to Intrinsic Factor cobalamin (Cbl-IF) with a high affinity and that is expressed in both kidney and ileal epithelial cells. Based on this observation, it has been speculated that cubilin and Intrinsic Factor cobalamin receptor (IFCR)
H. Schohn - One of the best experts on this subject based on the ideXlab platform.
-
Intrinsic Factor receptor during fetal development of the human intestine.
The Biochemical journal, 1992Co-Authors: H. Schohn, J.l. Guéant, G. Grignon, B Leheup, M Saunier, J. P. NicolasAbstract:Intrinsic Factor receptor activity was observed in mucosal homogenates from whole small intestine and colon of 10-19-week fetuses, whereas it was only detected in the distal part of the small intestine of a 25-week fetus. The receptor-Intrinsic Factor-cobalamin complex was eluted into the void-volume position when ileum mucosal extract was assayed for receptor activity by gel filtration after incubation with either fetal gastric extract or human gastric juice. The Intrinsic-Factor-binding capacity of intestinal mucosal extracts ranged from 2.6 to 30.5 fmol/mg and was correlated with the gestational age of six fetuses. The dissociation constant of the receptor for the Intrinsic Factor-cobalamin complex was estimated at 0.24-0.36 nM at pH 7.4. In conclusion, Intrinsic-Factor-receptor activity was detected in the whole intestine in 10-19-week fetuses, whereas it was only present in the distal ileum at the end of fetal development.
-
Binding assay and physicochemical characteristics of solubilized Intrinsic Factor receptor in ileal mucosal homogenates using phenyl-Sepharose to separate the saturated receptor from free Intrinsic Factor
Biochimica et biophysica acta, 1991Co-Authors: Jean-louis Guéant, H. Schohn, Ralph Gräsbeck, H. Brulé, Monique Saunier, Jean-pierre NicolasAbstract:A radioisotopic assay was set to determine the physicochemical properties of the solubilized Intrinsic Factor receptor in pig mucosal extracts. In this assay, phenyl-Sepharose was used to separate the receptor-Intrinsic Factor-labelled cobalamin complex from the free saturated Intrinsic Factor. The association constant (at pH 7.4) of the receptor-Intrinsic Factor complex was estimated at 3.4 +/- 0.3 nM-1. Adsorption of the apo-receptor to phenyl-Sepharose allowed its binding site to be made accessible to Intrinsic Factor with an association constant in order of 6 nM-1. The receptor binding activity obtained with five mucosal extracts was closely correlated with that obtained by gel filtration of the Intrinsic Factor-receptor complex (r = 0.99). The radioisotope assay was used to detect the unsaturated receptor (apo-receptor) in sucrose density ultracentrifugation and in superose 6 gel filtration. The sedimentation coefficient was 9.5 s. The apo-receptor was eluted in three peaks in gel filtration, corresponding to the formation of oligomers. The peak of the monomer was increased in presence of EDTA. Its molecular mass was estimated at 270 kDa and its Stokes radius at 5.9 nm. It was concluded that calcium is involved in the oligomerisation of the apo-receptor.
Jean-louis Guéant - One of the best experts on this subject based on the ideXlab platform.
-
Binding assay and physicochemical characteristics of solubilized Intrinsic Factor receptor in ileal mucosal homogenates using phenyl-Sepharose to separate the saturated receptor from free Intrinsic Factor
Biochimica et biophysica acta, 1991Co-Authors: Jean-louis Guéant, H. Schohn, Ralph Gräsbeck, H. Brulé, Monique Saunier, Jean-pierre NicolasAbstract:A radioisotopic assay was set to determine the physicochemical properties of the solubilized Intrinsic Factor receptor in pig mucosal extracts. In this assay, phenyl-Sepharose was used to separate the receptor-Intrinsic Factor-labelled cobalamin complex from the free saturated Intrinsic Factor. The association constant (at pH 7.4) of the receptor-Intrinsic Factor complex was estimated at 3.4 +/- 0.3 nM-1. Adsorption of the apo-receptor to phenyl-Sepharose allowed its binding site to be made accessible to Intrinsic Factor with an association constant in order of 6 nM-1. The receptor binding activity obtained with five mucosal extracts was closely correlated with that obtained by gel filtration of the Intrinsic Factor-receptor complex (r = 0.99). The radioisotope assay was used to detect the unsaturated receptor (apo-receptor) in sucrose density ultracentrifugation and in superose 6 gel filtration. The sedimentation coefficient was 9.5 s. The apo-receptor was eluted in three peaks in gel filtration, corresponding to the formation of oligomers. The peak of the monomer was increased in presence of EDTA. Its molecular mass was estimated at 270 kDa and its Stokes radius at 5.9 nm. It was concluded that calcium is involved in the oligomerisation of the apo-receptor.
