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人红细胞糖蛋白氨基的修饰以及M和N血型特异性结构基础的新概念

Modification of amino groups of human-erythrocyte glycoproteins and the new concept on the structural basis of M and M blood-group specificity.

作者信息

Lisowska E, Duk M

出版信息

Eur J Biochem. 1975 Jun;54(2):469-74. doi: 10.1111/j.1432-1033.1975.tb04158.x.

DOI:10.1111/j.1432-1033.1975.tb04158.x
PMID:1236795
Abstract
  1. Various kinds of modification of amino groups of M and N blood group glycoproteins abolished their capacity to inhibit rabbit and human anti-M and anit-N sera. 2. The reversible modification of amino groups revealed that M and N blood group activity was restored after the removal of amino-group-blocking residues. 3. Modification of amino groups had an entirely different effect on the reactivity of red cell glycoproteins with Vicia graminea agglutinin. The serological activity of N glycoprotein towards Vicia graminea anti-N agglutinin was unchanged, whereas the weak activity of M glycoprotein towards this anti-N agglutinin was increased to the level of the of N glycoprotein. 4. These results indicate that there is a structural difference between M and N glycoproteins, which resides beyond the oligosaccharide chains. It suggests in turn that M and N blood group specificity is determined by amino acid sequence in the peptide chains of red cell glycoproteins.
摘要
  1. 对M和N血型糖蛋白氨基进行的各种修饰消除了它们抑制兔和人抗M及抗N血清的能力。2. 氨基的可逆修饰表明,去除氨基阻断残基后,M和N血型活性得以恢复。3. 氨基修饰对红细胞糖蛋白与蚕豆凝集素的反应性产生了完全不同的影响。N糖蛋白对蚕豆抗N凝集素的血清学活性未变,而M糖蛋白对这种抗N凝集素的微弱活性则提高到了N糖蛋白的水平。4. 这些结果表明,M和N糖蛋白之间存在结构差异,该差异存在于寡糖链之外。这进而表明,M和N血型特异性由红细胞糖蛋白肽链中的氨基酸序列决定。

相似文献

1
Modification of amino groups of human-erythrocyte glycoproteins and the new concept on the structural basis of M and M blood-group specificity.人红细胞糖蛋白氨基的修饰以及M和N血型特异性结构基础的新概念
Eur J Biochem. 1975 Jun;54(2):469-74. doi: 10.1111/j.1432-1033.1975.tb04158.x.
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Vicia graminea anti-N lectin: partial characterization of the purified lectin and its binding to erythrocytes.细叶野豌豆抗N凝集素:纯化凝集素的部分特性及其与红细胞的结合
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Effect of pH on the binding of Vicia graminea lectin to erythrocytes. Dependence on the chemical character of red-cell receptors.pH对野豌豆凝集素与红细胞结合的影响。对红细胞受体化学特性的依赖性。
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The amino acid sequence of the Mc-specific major red cell membrane sialoglycoprotein--an intermediate of the blood group M- and N-active molecules.Mc特异性主要红细胞膜唾液糖蛋白的氨基酸序列——血型M和N活性分子的中间体。
Hoppe Seylers Z Physiol Chem. 1981 Mar;362(3):363-6.

引用本文的文献

1
Ss blood group associated PAS-staining polymorphism of glycoprotein 3 from human erythrocyte membranes.
Hum Genet. 1976 May 19;32(2):121-32. doi: 10.1007/BF00291494.
2
Self-digestion of human erythrocyte membranes. Role of adenosine triphosphate and glutathione.人红细胞膜的自消化。三磷酸腺苷和谷胱甘肽的作用。
Biochem J. 1977 May 15;164(2):469-72. doi: 10.1042/bj1640469.
3
Different N-terminal amino acids in the MN-glycoprotein from MM and NN erythrocytes.来自MM型和NN型红细胞的MN糖蛋白中不同的N端氨基酸。
Hum Genet. 1977 Mar 14;35(3):335-43. doi: 10.1007/BF00446624.
4
Three-dimensional model of highly M-active NH2-terminal sialoglycopentapeptide from human blood group MM red cells.来自人类血型MM红细胞的高M活性NH2末端唾液酸糖五肽的三维模型。
Naturwissenschaften. 1978 Oct;65(10):547-8. doi: 10.1007/BF00439809.
5
Isolation and structural characterization of alkali-labile oligosaccharides from bovine milk-fat-globule membrane.牛乳脂肪球膜中碱不稳定寡糖的分离与结构表征
Biochem J. 1978 Jun 1;171(3):549-57. doi: 10.1042/bj1710549.
6
[Glycoproteins: their biological and clinical significance. II (author's transl)].[糖蛋白:它们的生物学和临床意义。II(作者译)]
Klin Wochenschr. 1979 Mar 1;57(5):199-214. doi: 10.1007/BF01477489.
7
[Biology of lectins and their application in clinical biochemistry (author's transl)].[凝集素的生物学及其在临床生物化学中的应用(作者译)]
Klin Wochenschr. 1977 Apr 15;55(8):359-73. doi: 10.1007/BF01488621.
8
Studies on the receptors of the MNSs group system.MNSs血型系统受体的研究
Blut. 1976 Mar;32(3):163-70. doi: 10.1007/BF00995909.