Complete amino-acid sequence of bovine seminal ribonuclease, a dimeric protein from seminal plasma.
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.
Suzuki
H
H
Dipartimento di Chimica Organica e Biologica, Universita' di Napoli.
Parente
A
A
Farina
B
B
Greco
L
L
La Montagna
R
R
Leone
E
E
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002918:Chymotrypsin; D006868:Hydrolysis; D008297:Male; D008969:Molecular Sequence Data; D010455:Peptides / Q000032:analysis; D012260:Ribonucleases / Q000032:analysis*; D012661:Semen / Q000201:enzymology*; D014357:Trypsin
D010455:Peptides; D012260:Ribonucleases; D002918:Chymotrypsin; D014357:Trypsin