| First Author | Murayama J | Year | 1989 |
| Journal | Biochim Biophys Acta | Volume | 999 |
| Pages | 273-80 | PubMed ID | 2605264 |
| Abstract Text | A major sialoglycoprotein, glycophorin MK, was isolated from monkey erythrocyte membranes by extraction with lithium diiodosalicylate and partition in aqueous phenol. Chemical analysis of glycophorin MK revealed that the glycophorin consists of 51% protein and 49% carbohydrate by weight, and contains no N-glycosidic oligosaccharide units. Only N-glycolylneuraminic acid (Neu5Gc) was detected as sialic acid. The amino acid sequence of glycophorin MK was determined, which demonstrated that the glycophorin consists of 144 amino acid residues and 18 oligosaccharide units linked O-glycosidically to the peptide backbone through serine or threonine residues. The molecular weight was estimated to be about 35,000 based on the amino acid residues and carbohydrate content. By comparison of the amino acid sequence with those of human, equine and porcine glycophorins, a striking sequence homology was observed between monkey and human glycophorin. Glycophorin MK demonstrated both M and N blood group activities. | Doi | 10.1016/0167-4838(89)90009-5 |
| Issue | 3 | Month | Dec |
