Title :
Glycophorins B and C from human erythrocyte membranes
Abstract :
- Purification and sequence analysis
- We have developed methods for the preparative purification of two sialoglycoproteins ( glycophorins B and C ) from human erythrocyte membranes by high-performance ion exchange and gel permeation chromatography in the presence of Triton X-100
- Glycophorin B was obtained without any detectable contaminants, and glycophorin C exhibited a purity of about 90-95%
- The amino acid sequence of the intramembranous domain ( residues 36-71 ) of glycophorin B was determined and found to be similar to that of the hydrophobic region of the major sialoglycoprotein ( glycophorin A )
- The amino acid sequence of the hydrophobic domain ( residues 49-88 ) of glycophorin C , that was also determined, agreed completely with the structure recently deduced from cDNA sequencing
Output (sent_index, trigger,
protein,
sugar,
site):
- 2. sialoglycoproteins, , glycophorins B and C, -, -
- 2. sialoglycoproteins, , sialoglycoproteins, -, -
- 4. sialoglycoprotein, , glycophorin A, -, -
- 4. sialoglycoprotein, , sialoglycoprotein, -, -
Output(Part-Of) (sent_index,
protein,
site):
- 4. glycophorin B, domain
- 4. glycophorin B, residues 36-71
- 4. sialoglycoprotein, region
- 5. glycophorin C, domain
- 5. glycophorin C, residues 49-88
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):