Abstract
Glycophorin was prepared from dog erythrocyte membranes by extraction with lithium diiodosalicylate and partition in aqueous phenol. Tryptic and chymotryptic treatments of the glycophorin produced two major glycopeptides labeled T1 and CH1, respectively. The glycopeptides were isolated by gel chromatography followed by ion-exchange chromatography, and subjected to amino acid sequence analysis. Both glycopeptides represented the amino-terminal domain of the major dog glycophorin; T1 of 52 residues and CH1 of 43 residues. The amino-terminal sequence of dog glycophorin does not have significant homology with those of human, horse or porcine glycophorins. This result is in good agreement with our previous proposal that there is no homology in the sequence of the amino-terminal glycosylated domain of glycophorin.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
