Title : Structural studies on rat
prostatic binding protein
Abstract :
- The primary structure of its glycosylated component C3
- The amino acid sequence of the glycosylated component C3 of rat prostatic binding protein has been determined
- The peptides obtained by digestion of the S-carboxamidomethylated or S-aminoethylated glycoprotein with trypsin and Staphylococcus aureus protease were sequenced by manual Edman degradation
- The alignment of the fragments was further established with overlapping peptides obtained by enzymic hydrolysis of the modified protein with chymotrypsin and thermolysin , and by chemical cleavage with cyanogen bromide
- The glycopeptide C3 contains 77 amino acids corresponding to a molecular weight of 8653
- the oligosaccharide chain is attached to the peptide by an N-glycosidic bond to asparagine-17
- C3 is an acidic polypeptide due to the presence of ten acidic residues ; its three cysteine residues are located at both extremities and in the middle of the molecule
Output (sent_index, trigger,
protein,
sugar,
site):
- 3. glycoprotein, , glycoprotein, -, -
- 5. glycopeptide, , -, -, glycopeptide
- 6. attached, , -, the oligosaccharide chain, peptide
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):