Primary defect of congenital dyserythropoietic anemia type II. Failure in glycosylation of erythrocyte lactosaminoglycan proteins caused by lowered N-acetylglucosaminyltransferase II.-Reference-Cited by-同舟云学术

Primary defect of congenital dyserythropoietic anemia type II. Failure in glycosylation of erythrocyte lactosaminoglycan proteins caused by lowered N-acetylglucosaminyltransferase II.

Published:1987-05 Issue:15 Volume:262 Page:7195-7206
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Fukuda M N,Dell A,Scartezzini P

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference59 articles.

1. Developmental change and genetic defect in the carbohydrate structure of band 3 glycoprotein of human erythrocyte membrane.

2. Erythroglycan, a high molecular weight glycopeptide with the repeating structure [galactosyl-(1 leads to 4)-2-deoxy-2-acetamido-glucosyl(1 leads to 3)] comprising more than one-third of the protein-bound carbohydrate of human erythrocyte stroma.

3. Alkali-stable blood group A- and B-active poly(glycosyl)-peptides from human erythrocyte membrane

4. Cell surface carbohydrates of embryonal carcinoma cells: Polysaccharidic side chains of F9 antigens and of receptors to two lectins, FBP and PNA

5. Isolation and characterization of polyfucosylated lactosaminoglycan from human granulocytes.

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