Physico-chemical properties and evidence for electrophoretic variants of rat transcortin

Hormonal effects on the secretion and glycoform profile of corticosteroid-binding globulin

“…This discrepancy is most likely due to differences in the pH gradient of IPG strips from different manufacturers, since a control sample focussed on an Amersham IPG strip showed a pI range of 4.2-4.8. The electrophoretic doublet usually observed for CBG [9] in 1D-PAGE was also discernable in 2D-PAGE. These findings suggest that HepG2 cells are capable of producing most, if not all, CBG glycoforms usually found in human blood.…”

“…Intact CBG consists of two broad electrophoretic variants [9] and up to 13 isoforms that can be resolved by twodimensional polyacrylamide gel-electrophoresis (2D-PAGE) [10,11]. The appearance of these different isoforms is most likely due to differences in glycosylation.…”

Hormonal effects on the secretion and glycoform profile of corticosteroid-binding globulin

“…This discrepancy is most likely due to differences in the pH gradient of IPG strips from different manufacturers, since a control sample focussed on an Amersham IPG strip showed a pI range of 4.2-4.8. The electrophoretic doublet usually observed for CBG [9] in 1D-PAGE was also discernable in 2D-PAGE. These findings suggest that HepG2 cells are capable of producing most, if not all, CBG glycoforms usually found in human blood.…”

“…Intact CBG consists of two broad electrophoretic variants [9] and up to 13 isoforms that can be resolved by twodimensional polyacrylamide gel-electrophoresis (2D-PAGE) [10,11]. The appearance of these different isoforms is most likely due to differences in glycosylation.…”

Enhanced corticosterone-binding capacity in plasma after stimulation of the rat adrenal cortex: the possibility of a simultaneous release of protein and corticosterone

“…While Wolf et al (1981) felt that the observed heterogeneity reflected differences in the glycosylated portion of CBG, they did not rule out the possibility that a CBG-like pro¬ tein may be synthesized in organs other than the liver and thus account for the second protein moiety in the plasma. Favre, Le Gaillard, Mattret-Turrion et al (1984) found that rat plasma transcortin migrated as a double band, whether free or bound to corticosterone.…”

Hormonal effects on the secretion and glycoform profile of corticosteroid-binding globulin

“…This discrepancy is most likely due to differences in the pH gradient of IPG strips from different manufacturers, since a control sample focussed on an Amersham IPG strip showed a pI range of 4.2-4.8. The electrophoretic doublet usually observed for CBG [9] in 1D-PAGE was also discernable in 2D-PAGE. These findings suggest that HepG2 cells are capable of producing most, if not all, CBG glycoforms usually found in human blood.…”

“…Intact CBG consists of two broad electrophoretic variants [9] and up to 13 isoforms that can be resolved by twodimensional polyacrylamide gel-electrophoresis (2D-PAGE) [10,11]. The appearance of these different isoforms is most likely due to differences in glycosylation.…”

Enhanced corticosterone-binding capacity in plasma after stimulation of the rat adrenal cortex: the possibility of a simultaneous release of protein and corticosterone

“…While Wolf et al (1981) felt that the observed heterogeneity reflected differences in the glycosylated portion of CBG, they did not rule out the possibility that a CBG-like pro¬ tein may be synthesized in organs other than the liver and thus account for the second protein moiety in the plasma. Favre, Le Gaillard, Mattret-Turrion et al (1984) found that rat plasma transcortin migrated as a double band, whether free or bound to corticosterone.…”

Hormonal effects on the secretion and glycoform profile of corticosteroid-binding globulin

“…This discrepancy is most likely due to differences in the pH gradient of IPG strips from different manufacturers, since a control sample focussed on an Amersham IPG strip showed a pI range of 4.2-4.8. The electrophoretic doublet usually observed for CBG [9] in 1D-PAGE was also discernable in 2D-PAGE. These findings suggest that HepG2 cells are capable of producing most, if not all, CBG glycoforms usually found in human blood.…”

“…Intact CBG consists of two broad electrophoretic variants [9] and up to 13 isoforms that can be resolved by twodimensional polyacrylamide gel-electrophoresis (2D-PAGE) [10,11]. The appearance of these different isoforms is most likely due to differences in glycosylation.…”

Enhanced corticosterone-binding capacity in plasma after stimulation of the rat adrenal cortex: the possibility of a simultaneous release of protein and corticosterone

“…While Wolf et al (1981) felt that the observed heterogeneity reflected differences in the glycosylated portion of CBG, they did not rule out the possibility that a CBG-like pro¬ tein may be synthesized in organs other than the liver and thus account for the second protein moiety in the plasma. Favre, Le Gaillard, Mattret-Turrion et al (1984) found that rat plasma transcortin migrated as a double band, whether free or bound to corticosterone.…”