The Experts below are selected from a list of 2031 Experts worldwide ranked by ideXlab platform
Taei Matsui - One of the best experts on this subject based on the ideXlab platform.
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Structures of the Asparagine-Linked Oligosaccharide chains of human von Willebrand factor. Occurrence of blood group A, B, and H(O) structures.
The Journal of biological chemistry, 1992Co-Authors: Taei Matsui, Koiti Titani, Tsuguo MizuochiAbstract:Abstract The Asparagine-Linked Oligosaccharide chains of human von Willebrand factor (vWF) purified from pooled plasma were quantitatively liberated from the polypeptide moiety by hydrazinolysis. After N-acetylation, these were fractionated by paper electrophoresis and sequential chromatography on lectin-affinity columns of concanavalin A, Phaseolus vulgaris erythrophytohemagglutinin, Datura stramonium agglutinin, Ricinus communis agglutinin 120, and Ulex europaeus agglutinin I and on a Bio-Gel P-4 column. Their structures were investigated by sequential exoglycosidase digestion in conjunction with methylation analysis. The glycoprotein was shown to be unique in its great diversity of Oligosaccharide structures. Another noteworthy finding which had not been reported previously was the occurrence of Asparagine-Linked Oligosaccharide chains with blood group A, B, and H(O) structures. In the present study, this glycoprotein was shown to contain mono- (0.4% of the total Oligosaccharides), bi-(78.2%), tri- (12.3%), and tetraantennary (2.3%) complex type Oligosaccharides in addition to a series of high mannose type Oligosaccharides, Man6-9GlcNAc2 (0.8%). Biantennary complex type Oligosaccharide chains were those with (8.2%) and without (70.0%) a bisecting GlcNAc residue and approximately 13.2%, 2.2%, and 0.4% of these contained blood group H(O), A, and B structures, respectively. The tri- and tetraantennary complex type chains were those with and without N-acetyllactosamine repeats, and about 13.0% of the triantennary chains without the N-acetyllactosamine repeat contained the blood group H(O) structure. Occurrence of these Asparagine-Linked Oligosaccharides with blood group A and B structures suggest that the repeated use of factor VIII/vWF pooled concentrate for the treatment of hemophiliacs could result in the production of antibodies against vWF with a different blood group from that of the patient, and this development may be pathogenic.
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Structures of the Asparagine-Linked Oligosaccharide Chains of Human von Willebrand Factor
1992Co-Authors: Taei Matsui, Koiti Titani, Tsuguo MizuochisAbstract:The Asparagine-Linked Oligosaccharide chains of human von Willebrand factor (vWF) purified from pooled plasma were quantitatively liberated from the polypeptide moiety by hydrazinolysis. After N-acetylation, these were fractionated by paper electrophoresis and sequential chromatography on lectin-affinity columns of concanavalin A, Phaseolus vulgaris erythrophytohemagglutinin, Datura stramonium agglutinin, Ricinus communis agglutinin 120, and Ulex europaeus agglutinin I and on a Bio-Gel P-4 column. Their structures were investigated by sequential exoglycosidase digestion in conjunction with methylation analysis. The glycoprotein was shown to be unique in its great diversity of Oligosaccharide structures. Another noteworthy finding which had not been reported previously was the occurrence of Asparagine-Linked Oligosaccharide chains with blood group A, B, and H(0) structures. In the present study, this glycoprotein was shown to contain mono- (0.4% of the total Oligosaccharides), bi(78.2%), tri- (12.3%), and tetraantennary (2.3%) complex type Oligosaccharides in addition to a series of high mannose type Oligosaccharides, Man6-9GlcNAc2 (0.8%). Biantennary complex type Oligosaccharide chains were those with (8.2%) and without (70.0%) a bisecting GlcNAc residue and approximately 13.2%, 2.2%, and 0.4% of these contained blood group H(O), A, and B structures, respectively. The tri- and tetraantennary complex type chains were those with and without N-acetyllactosamine repeats, and about 13.0% of the triantennary chains without the N-acetyllactosamine repeat contained the blood group H(0) structure. Occurrence of these Asparagine-Linked Oligosaccharides with blood group A and B structures suggest that the repeated use of factor VIII/vWF pooled concentrate for the treatment of hemophiliacs could result in the production of antibodies against vWF with a different blood group from that of the patient, and this development may be pathogenic.
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β subunits of equine chorionic gonadotropin and lutenizing hormone with an identical amino acid sequence have different Asparagine Linked Oligosaccharide chains
Biochemical and Biophysical Research Communications, 1991Co-Authors: Taei Matsui, George R. Bousfield, Darrell N Ward, Hiromu Sugino, Mari Miura, Koiti Titani, Tsuguo MizuochiAbstract:Abstract The glycoprotein hormones, equine chorionic gonadotropin (eCG) and lutenizing hormone (eLH), possess a β-subunit with an identical amino acid sequence. The Asn-Linked Oligosaccharide chains of eCGβ and eLHβ were quantitatively liberated as tritium-labeled Oligosaccharides by hydrazinolysis followed by N-acetylation and NaB3H4-reduction. Paper electrophoresis in combination with sialidase digestion and solvolytic desulfation indicated that eCGβ contained neutral and sialylated Oligosaccharides, while eLHβ contained neutral, sialylated, sulfated, and both sialylated and sulfated Oligosaccharides. In addition, elution profiles on a Bio-Gel P-4 column of the neutralized Oligosaccharide mixtures of eCGβ and eLHβ were different, indicating that the molecular masses of Oligosaccharides of the two glycoproteins are different. Therefore, this suggests that the structures of the Asn-Linked Oligosaccharide chains of eCGβ and eLHβ are different although they have an identical amino acid sequence.
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β subunits of equine chorionic gonadotropin and lutenizing hormone with an identical amino acid sequence have different Asparagine Linked Oligosaccharide chains
Biochemical and Biophysical Research Communications, 1991Co-Authors: Taei Matsui, George R. Bousfield, Darrell N Ward, Hiromu Sugino, Mari Miura, Koiti Titani, Tsuguo MizuochiAbstract:The glycoprotein hormones, equine chorionic gonadotropin (eCG) and lutenizing hormone (eLH), possess a beta-subunit with an identical amino acid sequence. The Asn-Linked Oligosaccharide chains of eCG beta and eLH beta were quantitatively liberated as tritium-labeled Oligosaccharides by hydrazinolysis followed by N-acetylation and NaB3H4-reduction. Paper electrophoresis in combination with sialidase digestion and solvolytic desulfation indicated that eCG beta contained neutral and sialylated Oligosaccharides, while eLH beta contained neutral, sialylated, sulfated, and both sialylated and sulfated Oligosaccharides. In addition, elution profiles on a Bio-Gel P-4 column of the neutralized Oligosaccharide mixtures of eCG beta and eLH beta were different, indicating that the molecular masses of Oligosaccharides of the two glycoproteins are different. Therefore, this suggests that the structures of the Asn-Linked Oligosaccharide chains of eCG beta and eLH beta are different although they have an identical amino acid sequence.
Tsuguo Mizuochi - One of the best experts on this subject based on the ideXlab platform.
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Structures of the Asparagine-Linked Oligosaccharide chains of human von Willebrand factor. Occurrence of blood group A, B, and H(O) structures.
The Journal of biological chemistry, 1992Co-Authors: Taei Matsui, Koiti Titani, Tsuguo MizuochiAbstract:Abstract The Asparagine-Linked Oligosaccharide chains of human von Willebrand factor (vWF) purified from pooled plasma were quantitatively liberated from the polypeptide moiety by hydrazinolysis. After N-acetylation, these were fractionated by paper electrophoresis and sequential chromatography on lectin-affinity columns of concanavalin A, Phaseolus vulgaris erythrophytohemagglutinin, Datura stramonium agglutinin, Ricinus communis agglutinin 120, and Ulex europaeus agglutinin I and on a Bio-Gel P-4 column. Their structures were investigated by sequential exoglycosidase digestion in conjunction with methylation analysis. The glycoprotein was shown to be unique in its great diversity of Oligosaccharide structures. Another noteworthy finding which had not been reported previously was the occurrence of Asparagine-Linked Oligosaccharide chains with blood group A, B, and H(O) structures. In the present study, this glycoprotein was shown to contain mono- (0.4% of the total Oligosaccharides), bi-(78.2%), tri- (12.3%), and tetraantennary (2.3%) complex type Oligosaccharides in addition to a series of high mannose type Oligosaccharides, Man6-9GlcNAc2 (0.8%). Biantennary complex type Oligosaccharide chains were those with (8.2%) and without (70.0%) a bisecting GlcNAc residue and approximately 13.2%, 2.2%, and 0.4% of these contained blood group H(O), A, and B structures, respectively. The tri- and tetraantennary complex type chains were those with and without N-acetyllactosamine repeats, and about 13.0% of the triantennary chains without the N-acetyllactosamine repeat contained the blood group H(O) structure. Occurrence of these Asparagine-Linked Oligosaccharides with blood group A and B structures suggest that the repeated use of factor VIII/vWF pooled concentrate for the treatment of hemophiliacs could result in the production of antibodies against vWF with a different blood group from that of the patient, and this development may be pathogenic.
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β subunits of equine chorionic gonadotropin and lutenizing hormone with an identical amino acid sequence have different Asparagine Linked Oligosaccharide chains
Biochemical and Biophysical Research Communications, 1991Co-Authors: Taei Matsui, George R. Bousfield, Darrell N Ward, Hiromu Sugino, Mari Miura, Koiti Titani, Tsuguo MizuochiAbstract:Abstract The glycoprotein hormones, equine chorionic gonadotropin (eCG) and lutenizing hormone (eLH), possess a β-subunit with an identical amino acid sequence. The Asn-Linked Oligosaccharide chains of eCGβ and eLHβ were quantitatively liberated as tritium-labeled Oligosaccharides by hydrazinolysis followed by N-acetylation and NaB3H4-reduction. Paper electrophoresis in combination with sialidase digestion and solvolytic desulfation indicated that eCGβ contained neutral and sialylated Oligosaccharides, while eLHβ contained neutral, sialylated, sulfated, and both sialylated and sulfated Oligosaccharides. In addition, elution profiles on a Bio-Gel P-4 column of the neutralized Oligosaccharide mixtures of eCGβ and eLHβ were different, indicating that the molecular masses of Oligosaccharides of the two glycoproteins are different. Therefore, this suggests that the structures of the Asn-Linked Oligosaccharide chains of eCGβ and eLHβ are different although they have an identical amino acid sequence.
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β subunits of equine chorionic gonadotropin and lutenizing hormone with an identical amino acid sequence have different Asparagine Linked Oligosaccharide chains
Biochemical and Biophysical Research Communications, 1991Co-Authors: Taei Matsui, George R. Bousfield, Darrell N Ward, Hiromu Sugino, Mari Miura, Koiti Titani, Tsuguo MizuochiAbstract:The glycoprotein hormones, equine chorionic gonadotropin (eCG) and lutenizing hormone (eLH), possess a beta-subunit with an identical amino acid sequence. The Asn-Linked Oligosaccharide chains of eCG beta and eLH beta were quantitatively liberated as tritium-labeled Oligosaccharides by hydrazinolysis followed by N-acetylation and NaB3H4-reduction. Paper electrophoresis in combination with sialidase digestion and solvolytic desulfation indicated that eCG beta contained neutral and sialylated Oligosaccharides, while eLH beta contained neutral, sialylated, sulfated, and both sialylated and sulfated Oligosaccharides. In addition, elution profiles on a Bio-Gel P-4 column of the neutralized Oligosaccharide mixtures of eCG beta and eLH beta were different, indicating that the molecular masses of Oligosaccharides of the two glycoproteins are different. Therefore, this suggests that the structures of the Asn-Linked Oligosaccharide chains of eCG beta and eLH beta are different although they have an identical amino acid sequence.
Koiti Titani - One of the best experts on this subject based on the ideXlab platform.
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Structures of the Asparagine-Linked Oligosaccharide chains of human von Willebrand factor. Occurrence of blood group A, B, and H(O) structures.
The Journal of biological chemistry, 1992Co-Authors: Taei Matsui, Koiti Titani, Tsuguo MizuochiAbstract:Abstract The Asparagine-Linked Oligosaccharide chains of human von Willebrand factor (vWF) purified from pooled plasma were quantitatively liberated from the polypeptide moiety by hydrazinolysis. After N-acetylation, these were fractionated by paper electrophoresis and sequential chromatography on lectin-affinity columns of concanavalin A, Phaseolus vulgaris erythrophytohemagglutinin, Datura stramonium agglutinin, Ricinus communis agglutinin 120, and Ulex europaeus agglutinin I and on a Bio-Gel P-4 column. Their structures were investigated by sequential exoglycosidase digestion in conjunction with methylation analysis. The glycoprotein was shown to be unique in its great diversity of Oligosaccharide structures. Another noteworthy finding which had not been reported previously was the occurrence of Asparagine-Linked Oligosaccharide chains with blood group A, B, and H(O) structures. In the present study, this glycoprotein was shown to contain mono- (0.4% of the total Oligosaccharides), bi-(78.2%), tri- (12.3%), and tetraantennary (2.3%) complex type Oligosaccharides in addition to a series of high mannose type Oligosaccharides, Man6-9GlcNAc2 (0.8%). Biantennary complex type Oligosaccharide chains were those with (8.2%) and without (70.0%) a bisecting GlcNAc residue and approximately 13.2%, 2.2%, and 0.4% of these contained blood group H(O), A, and B structures, respectively. The tri- and tetraantennary complex type chains were those with and without N-acetyllactosamine repeats, and about 13.0% of the triantennary chains without the N-acetyllactosamine repeat contained the blood group H(O) structure. Occurrence of these Asparagine-Linked Oligosaccharides with blood group A and B structures suggest that the repeated use of factor VIII/vWF pooled concentrate for the treatment of hemophiliacs could result in the production of antibodies against vWF with a different blood group from that of the patient, and this development may be pathogenic.
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Structures of the Asparagine-Linked Oligosaccharide Chains of Human von Willebrand Factor
1992Co-Authors: Taei Matsui, Koiti Titani, Tsuguo MizuochisAbstract:The Asparagine-Linked Oligosaccharide chains of human von Willebrand factor (vWF) purified from pooled plasma were quantitatively liberated from the polypeptide moiety by hydrazinolysis. After N-acetylation, these were fractionated by paper electrophoresis and sequential chromatography on lectin-affinity columns of concanavalin A, Phaseolus vulgaris erythrophytohemagglutinin, Datura stramonium agglutinin, Ricinus communis agglutinin 120, and Ulex europaeus agglutinin I and on a Bio-Gel P-4 column. Their structures were investigated by sequential exoglycosidase digestion in conjunction with methylation analysis. The glycoprotein was shown to be unique in its great diversity of Oligosaccharide structures. Another noteworthy finding which had not been reported previously was the occurrence of Asparagine-Linked Oligosaccharide chains with blood group A, B, and H(0) structures. In the present study, this glycoprotein was shown to contain mono- (0.4% of the total Oligosaccharides), bi(78.2%), tri- (12.3%), and tetraantennary (2.3%) complex type Oligosaccharides in addition to a series of high mannose type Oligosaccharides, Man6-9GlcNAc2 (0.8%). Biantennary complex type Oligosaccharide chains were those with (8.2%) and without (70.0%) a bisecting GlcNAc residue and approximately 13.2%, 2.2%, and 0.4% of these contained blood group H(O), A, and B structures, respectively. The tri- and tetraantennary complex type chains were those with and without N-acetyllactosamine repeats, and about 13.0% of the triantennary chains without the N-acetyllactosamine repeat contained the blood group H(0) structure. Occurrence of these Asparagine-Linked Oligosaccharides with blood group A and B structures suggest that the repeated use of factor VIII/vWF pooled concentrate for the treatment of hemophiliacs could result in the production of antibodies against vWF with a different blood group from that of the patient, and this development may be pathogenic.
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β subunits of equine chorionic gonadotropin and lutenizing hormone with an identical amino acid sequence have different Asparagine Linked Oligosaccharide chains
Biochemical and Biophysical Research Communications, 1991Co-Authors: Taei Matsui, George R. Bousfield, Darrell N Ward, Hiromu Sugino, Mari Miura, Koiti Titani, Tsuguo MizuochiAbstract:Abstract The glycoprotein hormones, equine chorionic gonadotropin (eCG) and lutenizing hormone (eLH), possess a β-subunit with an identical amino acid sequence. The Asn-Linked Oligosaccharide chains of eCGβ and eLHβ were quantitatively liberated as tritium-labeled Oligosaccharides by hydrazinolysis followed by N-acetylation and NaB3H4-reduction. Paper electrophoresis in combination with sialidase digestion and solvolytic desulfation indicated that eCGβ contained neutral and sialylated Oligosaccharides, while eLHβ contained neutral, sialylated, sulfated, and both sialylated and sulfated Oligosaccharides. In addition, elution profiles on a Bio-Gel P-4 column of the neutralized Oligosaccharide mixtures of eCGβ and eLHβ were different, indicating that the molecular masses of Oligosaccharides of the two glycoproteins are different. Therefore, this suggests that the structures of the Asn-Linked Oligosaccharide chains of eCGβ and eLHβ are different although they have an identical amino acid sequence.
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β subunits of equine chorionic gonadotropin and lutenizing hormone with an identical amino acid sequence have different Asparagine Linked Oligosaccharide chains
Biochemical and Biophysical Research Communications, 1991Co-Authors: Taei Matsui, George R. Bousfield, Darrell N Ward, Hiromu Sugino, Mari Miura, Koiti Titani, Tsuguo MizuochiAbstract:The glycoprotein hormones, equine chorionic gonadotropin (eCG) and lutenizing hormone (eLH), possess a beta-subunit with an identical amino acid sequence. The Asn-Linked Oligosaccharide chains of eCG beta and eLH beta were quantitatively liberated as tritium-labeled Oligosaccharides by hydrazinolysis followed by N-acetylation and NaB3H4-reduction. Paper electrophoresis in combination with sialidase digestion and solvolytic desulfation indicated that eCG beta contained neutral and sialylated Oligosaccharides, while eLH beta contained neutral, sialylated, sulfated, and both sialylated and sulfated Oligosaccharides. In addition, elution profiles on a Bio-Gel P-4 column of the neutralized Oligosaccharide mixtures of eCG beta and eLH beta were different, indicating that the molecular masses of Oligosaccharides of the two glycoproteins are different. Therefore, this suggests that the structures of the Asn-Linked Oligosaccharide chains of eCG beta and eLH beta are different although they have an identical amino acid sequence.
John C Fyfe - One of the best experts on this subject based on the ideXlab platform.
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cubilin expression and posttranslational modification in the canine gastrointestinal tract
American Journal of Physiology-gastrointestinal and Liver Physiology, 2000Co-Authors: Danbin Xu, John C FyfeAbstract:Cubilin is an endocytic receptor of the apical brush border membrane that is essential for intrinsic factor-mediated cobalamin absorption in small intestine. However, cubilin is more highly expressed in kidney and yolk sac, and recent molecular characterization of the receptor has focused on these tissues. The aim of this investigation was to examine tissue-specific cubilin expression and posttranslational modifications with an emphasis on the gastrointestinal tract. Intrinsic factor-cobalamin binding activity, cubilin immunoreactivity, and cubilin mRNA levels were determined in multiple segments of canine gastrointestinal mucosa and other tissues. These aspects of cubilin expression varied in parallel, suggesting that the major determinant of regional cubilin expression in the gastrointestinal tract is modulation of cubilin mRNA. Cell fractionation indicated that ileal cubilin is not strongly membrane associated. An ∼185-kDa brush border specific and two >400-kDa precursor forms of cubilin were identified. Asparagine-Linked Oligosaccharide modifications characterized by differential glycosidase digestion of affinity-purified cubilin from ileal mucosa and renal cortex differed, but ileal and renal intracellular cubilin comigrated on SDS-PAGE at ∼400 kDa after Oligosaccharide removal, thus reconciling previous conflicting size estimates of the cubilin polypeptide.
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Cubilin expression and posttranslational modification in the canine gastrointestinal tract.
American journal of physiology. Gastrointestinal and liver physiology, 2000Co-Authors: Danbin Xu, John C FyfeAbstract:Cubilin is an endocytic receptor of the apical brush border membrane that is essential for intrinsic factor-mediated cobalamin absorption in small intestine. However, cubilin is more highly expressed in kidney and yolk sac, and recent molecular characterization of the receptor has focused on these tissues. The aim of this investigation was to examine tissue-specific cubilin expression and posttranslational modifications with an emphasis on the gastrointestinal tract. Intrinsic factor-cobalamin binding activity, cubilin immunoreactivity, and cubilin mRNA levels were determined in multiple segments of canine gastrointestinal mucosa and other tissues. These aspects of cubilin expression varied in parallel, suggesting that the major determinant of regional cubilin expression in the gastrointestinal tract is modulation of cubilin mRNA. Cell fractionation indicated that ileal cubilin is not strongly membrane associated. An approximately 185-kDa brush border specific and two >400-kDa precursor forms of cubilin were identified. Asparagine-Linked Oligosaccharide modifications characterized by differential glycosidase digestion of affinity-purified cubilin from ileal mucosa and renal cortex differed, but ileal and renal intracellular cubilin comigrated on SDS-PAGE at approximately 400 kDa after Oligosaccharide removal, thus reconciling previous conflicting size estimates of the cubilin polypeptide.
Danbin Xu - One of the best experts on this subject based on the ideXlab platform.
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cubilin expression and posttranslational modification in the canine gastrointestinal tract
American Journal of Physiology-gastrointestinal and Liver Physiology, 2000Co-Authors: Danbin Xu, John C FyfeAbstract:Cubilin is an endocytic receptor of the apical brush border membrane that is essential for intrinsic factor-mediated cobalamin absorption in small intestine. However, cubilin is more highly expressed in kidney and yolk sac, and recent molecular characterization of the receptor has focused on these tissues. The aim of this investigation was to examine tissue-specific cubilin expression and posttranslational modifications with an emphasis on the gastrointestinal tract. Intrinsic factor-cobalamin binding activity, cubilin immunoreactivity, and cubilin mRNA levels were determined in multiple segments of canine gastrointestinal mucosa and other tissues. These aspects of cubilin expression varied in parallel, suggesting that the major determinant of regional cubilin expression in the gastrointestinal tract is modulation of cubilin mRNA. Cell fractionation indicated that ileal cubilin is not strongly membrane associated. An ∼185-kDa brush border specific and two >400-kDa precursor forms of cubilin were identified. Asparagine-Linked Oligosaccharide modifications characterized by differential glycosidase digestion of affinity-purified cubilin from ileal mucosa and renal cortex differed, but ileal and renal intracellular cubilin comigrated on SDS-PAGE at ∼400 kDa after Oligosaccharide removal, thus reconciling previous conflicting size estimates of the cubilin polypeptide.
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Cubilin expression and posttranslational modification in the canine gastrointestinal tract.
American journal of physiology. Gastrointestinal and liver physiology, 2000Co-Authors: Danbin Xu, John C FyfeAbstract:Cubilin is an endocytic receptor of the apical brush border membrane that is essential for intrinsic factor-mediated cobalamin absorption in small intestine. However, cubilin is more highly expressed in kidney and yolk sac, and recent molecular characterization of the receptor has focused on these tissues. The aim of this investigation was to examine tissue-specific cubilin expression and posttranslational modifications with an emphasis on the gastrointestinal tract. Intrinsic factor-cobalamin binding activity, cubilin immunoreactivity, and cubilin mRNA levels were determined in multiple segments of canine gastrointestinal mucosa and other tissues. These aspects of cubilin expression varied in parallel, suggesting that the major determinant of regional cubilin expression in the gastrointestinal tract is modulation of cubilin mRNA. Cell fractionation indicated that ileal cubilin is not strongly membrane associated. An approximately 185-kDa brush border specific and two >400-kDa precursor forms of cubilin were identified. Asparagine-Linked Oligosaccharide modifications characterized by differential glycosidase digestion of affinity-purified cubilin from ileal mucosa and renal cortex differed, but ileal and renal intracellular cubilin comigrated on SDS-PAGE at approximately 400 kDa after Oligosaccharide removal, thus reconciling previous conflicting size estimates of the cubilin polypeptide.
