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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1982-10-21
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pubmed:abstractText |
We report a study of HEMPAS erythrocyte membrane glycoproteins in relation to proteolytic digestion and surface labelling with galactose-oxidase/NaB[3H]4. The proteolytic digestion of band 3, the major intrinsic glycoprotein of the human erythrocyte membrane, reveals an abnormality in the outer glycosylated segment of this protein. 3H incorporation in band 3 and band 4.5 glycoproteins after treatment with galactose-oxidase/NaB[3H]4 is reduced in HEMPAS red cells suggesting a defective glycosylation of these proteins. These findings together with the persistence of i antigen and the normal presence of I antigen lead us to conclude that erythroblastic membrane features may persist in HEMPAS erythrocytes.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0007-1048
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pubmed:author |
|
|
pubmed:issnType |
Print
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pubmed:volume |
51
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
569-76
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:7104237-Adult,
pubmed-meshheading:7104237-Anemia, Dyserythropoietic, Congenital,
pubmed-meshheading:7104237-Anemia, Hemolytic, Congenital,
pubmed-meshheading:7104237-Borohydrides,
pubmed-meshheading:7104237-Child,
pubmed-meshheading:7104237-Chymotrypsin,
pubmed-meshheading:7104237-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:7104237-Erythrocyte Membrane,
pubmed-meshheading:7104237-Erythrocytes,
pubmed-meshheading:7104237-Galactose Oxidase,
pubmed-meshheading:7104237-Glycoproteins,
pubmed-meshheading:7104237-Humans,
pubmed-meshheading:7104237-Tritium,
pubmed-meshheading:7104237-Trypsin
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pubmed:year |
1982
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pubmed:articleTitle |
Decreased glycosylation of band 3 and band 4.5 glycoproteins of erythrocyte membrane in congenital dyserythropoietic anaemia type II.
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pubmed:publicationType |
Journal Article
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