Glycophorin

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Glycophorin A
PDB 1afo EBI.jpg
dimeric transmembrane domain of human glycophorin a, nmr, 20 structures
Identifiers
Symbol Glycophorin_A
Pfam PF01102
InterPro IPR001195
PROSITE PDOC00281
SCOP 1afo
SUPERFAMILY 1afo
OPM superfamily 25
OPM protein 1afo

A Glycophorin is a sialoglycoprotein of the membrane of a red blood cell. It is a membrane-spanning protein and carries sugar molecules. It is heavily glycosylated (60%). Glycophorins are rich in sialic acid, which gives the red blood cells a very hydrophilic-charged coat. This enables them to circulate without adhering to other cells or vessel walls.

Identification[edit]

After separation of red cell membranes by SDS-polyacrylamide gel electrophoresis and staining with periodic acid-Schiff staining (PAS), four glycophorins have been identified. These have been named glycophorin A, B, C, and D in order of the quantity present in the membrane, gylycophorin A being the most and glycophorin D the least common. A fifth (glycophorin E) has been identified within the human genome but cannot easily be detected on routine gel staining. In total, the glycophorins constitute ~2% of the total erythrocyte membrane protein mass. These proteins are also known under different nomenclatures but they are probably best known as the glycophorins.

Family members[edit]

The following four human genes encode glycophorin proteins:

Glycophorin D is now known to be a variant of Glycophorin C.

References[edit]

External links[edit]