Activation Peptide of Human Factor IX Has Oligosaccharides O-Glycosidically Linked to Threonine Residues at 159 and 169

Kishan Lal Agarwala, Shun-Ichiro Kawabata, Hitoshi Nishimura, Sadaaki Iwanaga, Toshifumi Takao, Hiroshi Murata, Yasutsugu Shimonishi

研究成果: ジャーナルへの寄稿記事

40 引用 (Scopus)

抄録

O-Linked oligosaccharide chains were identified in the activation peptide (AP) of human blood coagulation factor IX. The peptide obtained from human factor IX was separated into three molecular species (APα, AP β, and ??γ) by reversed-phase high-performance liquid chromatography. Amino acid analysis showed that APα, but not AP β and ??γ, contained galactosamine in addition to glucosamine, thereby suggesting the presence of an O-linked sugar chain(s) in the molecule of APa. A nonapeptide (APα-D4, residues 157–165) and an undecapeptide (APα-D5, 166–176) derived from APa contained Thr-159 and Thr-169, neither of which could be identified using a gas-phase protein sequencer. All other serine and threonine residues present in APα were identified by peptide sequencing. Component sugar and sialic acid analyses of APα-D4 and APα-D5 revealed that they contained 1 mol each of TV-acetyl-D-galactosamine (GalNAc), D-galactose (Gal), and sialic acid. Fast atom bombardment tandem mass spectrometric analysis of APα-D4 suggested the existence of Gal-GalNAc-Thr, NeuNAc-(Gal-)GalNAc-Thr, and NeuNAc-Gal-GalNAc-Thr structures. On the basis of amino acid analysis after the isolation of APα, it accounted for approximately 35% of the total activation peptide obtained. From these results, it was concluded that a part of the activation peptide of human factor IX in circulating blood has tri- and tetrasaccharides O-glycosidically linked to the threonine residues at 159 and 169.

元の言語英語
ページ(範囲)5167-5171
ページ数5
ジャーナルBiochemistry
33
発行部数17
DOI
出版物ステータス出版済み - 5 1 1994

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Factor IX
Threonine
Human engineering
Oligosaccharides
Chemical activation
Peptides
Activation Analysis
Galactosamine
N-Acetylneuraminic Acid
Sugars
Trisaccharides
Amino Acids
Glucosamine
High performance liquid chromatography
Reverse-Phase Chromatography
Galactose

All Science Journal Classification (ASJC) codes

  • Biochemistry

これを引用

Activation Peptide of Human Factor IX Has Oligosaccharides O-Glycosidically Linked to Threonine Residues at 159 and 169. / Agarwala, Kishan Lal; Kawabata, Shun-Ichiro; Nishimura, Hitoshi; Iwanaga, Sadaaki; Takao, Toshifumi; Murata, Hiroshi; Shimonishi, Yasutsugu.

:: Biochemistry, 巻 33, 番号 17, 01.05.1994, p. 5167-5171.

研究成果: ジャーナルへの寄稿記事

Agarwala, KL, Kawabata, S-I, Nishimura, H, Iwanaga, S, Takao, T, Murata, H & Shimonishi, Y 1994, 'Activation Peptide of Human Factor IX Has Oligosaccharides O-Glycosidically Linked to Threonine Residues at 159 and 169', Biochemistry, 巻. 33, 番号 17, pp. 5167-5171. https://doi.org/10.1021/bi00183a021
Agarwala, Kishan Lal ; Kawabata, Shun-Ichiro ; Nishimura, Hitoshi ; Iwanaga, Sadaaki ; Takao, Toshifumi ; Murata, Hiroshi ; Shimonishi, Yasutsugu. / Activation Peptide of Human Factor IX Has Oligosaccharides O-Glycosidically Linked to Threonine Residues at 159 and 169. :: Biochemistry. 1994 ; 巻 33, 番号 17. pp. 5167-5171.
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title = "Activation Peptide of Human Factor IX Has Oligosaccharides O-Glycosidically Linked to Threonine Residues at 159 and 169",
abstract = "O-Linked oligosaccharide chains were identified in the activation peptide (AP) of human blood coagulation factor IX. The peptide obtained from human factor IX was separated into three molecular species (APα, AP β, and ??γ) by reversed-phase high-performance liquid chromatography. Amino acid analysis showed that APα, but not AP β and ??γ, contained galactosamine in addition to glucosamine, thereby suggesting the presence of an O-linked sugar chain(s) in the molecule of APa. A nonapeptide (APα-D4, residues 157–165) and an undecapeptide (APα-D5, 166–176) derived from APa contained Thr-159 and Thr-169, neither of which could be identified using a gas-phase protein sequencer. All other serine and threonine residues present in APα were identified by peptide sequencing. Component sugar and sialic acid analyses of APα-D4 and APα-D5 revealed that they contained 1 mol each of TV-acetyl-D-galactosamine (GalNAc), D-galactose (Gal), and sialic acid. Fast atom bombardment tandem mass spectrometric analysis of APα-D4 suggested the existence of Gal-GalNAc-Thr, NeuNAc-(Gal-)GalNAc-Thr, and NeuNAc-Gal-GalNAc-Thr structures. On the basis of amino acid analysis after the isolation of APα, it accounted for approximately 35{\%} of the total activation peptide obtained. From these results, it was concluded that a part of the activation peptide of human factor IX in circulating blood has tri- and tetrasaccharides O-glycosidically linked to the threonine residues at 159 and 169.",
author = "Agarwala, {Kishan Lal} and Shun-Ichiro Kawabata and Hitoshi Nishimura and Sadaaki Iwanaga and Toshifumi Takao and Hiroshi Murata and Yasutsugu Shimonishi",
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T1 - Activation Peptide of Human Factor IX Has Oligosaccharides O-Glycosidically Linked to Threonine Residues at 159 and 169

AU - Agarwala, Kishan Lal

AU - Kawabata, Shun-Ichiro

AU - Nishimura, Hitoshi

AU - Iwanaga, Sadaaki

AU - Takao, Toshifumi

AU - Murata, Hiroshi

AU - Shimonishi, Yasutsugu

PY - 1994/5/1

Y1 - 1994/5/1

N2 - O-Linked oligosaccharide chains were identified in the activation peptide (AP) of human blood coagulation factor IX. The peptide obtained from human factor IX was separated into three molecular species (APα, AP β, and ??γ) by reversed-phase high-performance liquid chromatography. Amino acid analysis showed that APα, but not AP β and ??γ, contained galactosamine in addition to glucosamine, thereby suggesting the presence of an O-linked sugar chain(s) in the molecule of APa. A nonapeptide (APα-D4, residues 157–165) and an undecapeptide (APα-D5, 166–176) derived from APa contained Thr-159 and Thr-169, neither of which could be identified using a gas-phase protein sequencer. All other serine and threonine residues present in APα were identified by peptide sequencing. Component sugar and sialic acid analyses of APα-D4 and APα-D5 revealed that they contained 1 mol each of TV-acetyl-D-galactosamine (GalNAc), D-galactose (Gal), and sialic acid. Fast atom bombardment tandem mass spectrometric analysis of APα-D4 suggested the existence of Gal-GalNAc-Thr, NeuNAc-(Gal-)GalNAc-Thr, and NeuNAc-Gal-GalNAc-Thr structures. On the basis of amino acid analysis after the isolation of APα, it accounted for approximately 35% of the total activation peptide obtained. From these results, it was concluded that a part of the activation peptide of human factor IX in circulating blood has tri- and tetrasaccharides O-glycosidically linked to the threonine residues at 159 and 169.

AB - O-Linked oligosaccharide chains were identified in the activation peptide (AP) of human blood coagulation factor IX. The peptide obtained from human factor IX was separated into three molecular species (APα, AP β, and ??γ) by reversed-phase high-performance liquid chromatography. Amino acid analysis showed that APα, but not AP β and ??γ, contained galactosamine in addition to glucosamine, thereby suggesting the presence of an O-linked sugar chain(s) in the molecule of APa. A nonapeptide (APα-D4, residues 157–165) and an undecapeptide (APα-D5, 166–176) derived from APa contained Thr-159 and Thr-169, neither of which could be identified using a gas-phase protein sequencer. All other serine and threonine residues present in APα were identified by peptide sequencing. Component sugar and sialic acid analyses of APα-D4 and APα-D5 revealed that they contained 1 mol each of TV-acetyl-D-galactosamine (GalNAc), D-galactose (Gal), and sialic acid. Fast atom bombardment tandem mass spectrometric analysis of APα-D4 suggested the existence of Gal-GalNAc-Thr, NeuNAc-(Gal-)GalNAc-Thr, and NeuNAc-Gal-GalNAc-Thr structures. On the basis of amino acid analysis after the isolation of APα, it accounted for approximately 35% of the total activation peptide obtained. From these results, it was concluded that a part of the activation peptide of human factor IX in circulating blood has tri- and tetrasaccharides O-glycosidically linked to the threonine residues at 159 and 169.

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U2 - 10.1021/bi00183a021

DO - 10.1021/bi00183a021

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VL - 33

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JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 17

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