Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.1 (chymotrypsin)
 10,938 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
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PMID:Structural studies on rat prostatic binding protein. The primary structure of its glycosylated component C3. 701 18

The amino acid sequence of component C1, the polypeptide specific for subunit F of prostatic binding protein, the major secretory glycoprotein of the rat ventral prostate, has been determined. Its structure was established using the manual Edman degradation on the intact protein and on the most relevant fragments isolated from trypsin, chymotrypsin, thermolysin and Staphylococcus aureus protease digests of the 14C-labelled S-carboxamidomethylated component C1. Component C1 contains 88 amino acids corresponding to a molecular weight of 10246. It is an acidic polypeptide due to the presence of 17 acidic residues; its three cysteine residues are almost symmetrically distributed over the peptide chain. Highly polar regions are found in positions 17-27 and 37-47, while the C-terminal part of the molecule contains two hydrophobic segments.
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PMID:Structural studies on rat prostatic binding protein. The primary structure of component C1 from subunit F. 720 13