The Journal of membrane biology.
Publisher:
Springer.
Frequency: Twelve no. a year, 2012-
Country: United States
Language: English
Start Year:1969 -
ISSN:
0022-2631 (Print)
1432-1424 (Electronic)
0022-2631 (Linking)
1432-1424 (Electronic)
0022-2631 (Linking)
Impact Factor
2.4
2022
| NLM ID: | 0211301 |
| (DNLM): | J29600000(s) |
| (OCoLC): | 01799894 |
| Coden: | JMBBBO |
| LCCN: | 76023326 |
| Classification: | W1 JO76H |
Primary structure of horse erythrocyte glycophorin HA. Its amino acid sequence has a unique homology with those of human and porcine erythrocyte glycophorins. The complete amino acid sequence of the major sialoglycoproteins of horse erythrocyte membranes, glycophorin HA, was determined by manual sequencing methods, using tryptic, chymotryptic, and cyanogen bromide fragments. Glycophorin HA is a polypeptide chain of 120 amino acid residues and contains 10 oligosaccharide units attached to the amino-terminal side of the molecule. Its amino terminus is pyroglutamic acid. All of the oligosaccharides are linked O-glycosidically to threonine or serine residues. The amino acid sequence is consistent with the transmembrane orientation of glycophorins. There...