251. Complete amino-acid sequence of bovine seminal ribonuclease, a dimeric protein from seminal plasma.
- Author
-
Suzuki H, Parente A, Farina B, Greco L, La Montagna R, and Leone E
- Subjects
- Amino Acid Sequence, Animals, Cattle, Chymotrypsin, Hydrolysis, Male, Molecular Sequence Data, Peptides analysis, Trypsin, Ribonucleases analysis, Semen enzymology
- Abstract
The complete amino-acid sequence of BS-RNAse, a dimeric ribonuclease isolated from bovine seminal plasma, was determined. The reduced and S-carboxymethylated subunit chain of the enzyme was cleaved by trypsin and chymotrypsin. The resulting peptides, purified by cation-exchange chromatography were sequenced by dansyl-Edman, subtractive Edman degradation and carboxypeptidase A and B digestion. Chymotryptic peptides were used for the alignment. Automated Edman degradation of the native protein, through the N-terminal 41 amino-acid residues, completed the sequence information. The subunit chain of BS-RNAse, composed of 124 amino-acid residues, with a molecular mass of 13,610 Da, is highly homologous (81%) to pancreatic ribonuclease A. A good degree of homology (31%) was also found with human angiogenin. No N-linked carbohydrate-attachment sites, such as Asn-X-Ser/Thr, were found in the protein.
- Published
- 1987
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