Literature DB >> 949329

Abnormal carbohydrate composition of the major penetrating membrane protein of En(a-) human erythrocytes.

M J Tanner, R E Jenkins, D J Anstee, J R Clamp.   

Abstract

The major penetrating membrane glycoprotein (band 3) was isolated from En(a-) and normal human erythrocytes. The two proteins differed only in carbohydrate composition. Band 3 from En(a-) erythrocytes contained greater amounts of galactose and N-acetyl-glucosamine. The loss of the sialoglycoprotein sialotetrasaccharides in the En(a-) cell is not compensated by the appearance of these units in band 3 of En(a-) erythrocytes.

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Year:  1976        PMID: 949329      PMCID: PMC1172895          DOI: 10.1042/bj1550701

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  15 in total

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2.  Protein measurement with the Folin phenol reagent.

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3.  The organization of the major protein of the human erythrocyte membrane.

Authors:  D H Boxer; R E Jenkins; M J Tanner
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4.  Membrane proteins related to anion permeability of human red blood cells. I. Localization of disulfonic stilbene binding sites in proteins involved in permeation.

Authors:  Z I Cabantchik; A Rothstein
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5.  A second Finnish En(a-) propositus with anti-Ena.

Authors:  U Furuhjelm; H R Nevanlinna; A Pirkola
Journal:  Vox Sang       Date:  1973       Impact factor: 2.144

6.  Separation and some properties of the major proteins of the human erythrocyte membrane.

Authors:  M J Tanner; D H Boxer
Journal:  Biochem J       Date:  1972-09       Impact factor: 3.857

Review 7.  Analysis of glycoproteins.

Authors:  J R Clamp
Journal:  Biochem Soc Symp       Date:  1974

8.  Membrane structure: some general principles.

Authors:  M S Bretscher
Journal:  Science       Date:  1973-08-17       Impact factor: 47.728

9.  Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin.

Authors:  M Tomita; V T Marchesi
Journal:  Proc Natl Acad Sci U S A       Date:  1975-08       Impact factor: 11.205

Review 10.  The organization of proteins in the human red blood cell membrane. A review.

Authors:  T L Steck
Journal:  J Cell Biol       Date:  1974-07       Impact factor: 10.539

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  14 in total

1.  Familial distal renal tubular acidosis is associated with mutations in the red cell anion exchanger (Band 3, AE1) gene.

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Review 2.  Oligomeric structure and the anion transport function of human erythrocyte band 3 protein.

Authors:  M L Jennings
Journal:  J Membr Biol       Date:  1984       Impact factor: 1.843

3.  Organization of membrane lipids and proteins in human En(a-) erythrocytes that lack the major sialoglycoprotein, glycophorin A. A spin-label study.

Authors:  S E Jansson; J Gripenberg; R Hekali; C G Gahmberg
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4.  Structure of the anion-transport protein of the human erythrocyte membrane. Further studies on the fragments produced by proteolytic digestion.

Authors:  D G Williams; R E Jenkins; M J Tanner
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5.  Red-cell glycophorin A-band 3 interactions associated with the movement of band 3 to the cell surface.

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6.  Differentiation of human erythroid cells is associated with increased O-glycosylation of the major sialoglycoprotein, glycophorin A.

Authors:  C G Gahmberg; M Ekblom; L C Andersson
Journal:  Proc Natl Acad Sci U S A       Date:  1984-11       Impact factor: 11.205

7.  Characterization and partial sequence of di-iodosulphophenyl isothiocyanate-binding peptide from human erythrocyte anion-transport protein.

Authors:  W J Mawby; J B Findlay
Journal:  Biochem J       Date:  1982-09-01       Impact factor: 3.857

8.  Genetic variants involving the major membrane sialoglycoprotein of human erythrocytes. Studies on erythrocytes of type Mk, Miltenberger class V and Mg.

Authors:  D J Anstee; M J Tanner
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9.  Glycophorin A interferes in the agglutination of human erythrocytes by concanavalin A. Explanation of the requirement for enzymic predigestion.

Authors:  S M Gokhale; N G Mehta
Journal:  Biochem J       Date:  1987-01-15       Impact factor: 3.857

Review 10.  Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.

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