The pairing of the four intrachain disulfide bonds of bovine se minal ribonuclease, a dimeric protein isolated from bovine seminal plasma, has been established by the isolation and characterization of the cystine peptides obtained from a thermolytic-tryptic hydrolysate of the protein. These disulfide bonds involve eight half-cystine residues located in the protein subunit chain at sequence positions identical with those of the eight half-cystine residues of the strictly homologous chain of bovine pancreatic ribonuclease. The results reported show that these eight 'homologous' half-cystine residues pair in seminal ribonuclease exactly as they do in pancreatic ribonuclease. They also indirectly confirm that the remaining two half-cystine residues present in each chain of the seminal enzyme are involved in intersubunit bonds
Intrachain Disulfide Bridges of Bovine Seminal Ribonuclease / DI DONATO, Alberto; D'Alessio, Giuseppe. - In: BIOCHIMICA ET BIOPHYSICA ACTA. - ISSN 0006-3002. - STAMPA. - 579:(1979), pp. 303-313.
Intrachain Disulfide Bridges of Bovine Seminal Ribonuclease
DI DONATO, ALBERTO;D'ALESSIO, GIUSEPPE
1979
Abstract
The pairing of the four intrachain disulfide bonds of bovine se minal ribonuclease, a dimeric protein isolated from bovine seminal plasma, has been established by the isolation and characterization of the cystine peptides obtained from a thermolytic-tryptic hydrolysate of the protein. These disulfide bonds involve eight half-cystine residues located in the protein subunit chain at sequence positions identical with those of the eight half-cystine residues of the strictly homologous chain of bovine pancreatic ribonuclease. The results reported show that these eight 'homologous' half-cystine residues pair in seminal ribonuclease exactly as they do in pancreatic ribonuclease. They also indirectly confirm that the remaining two half-cystine residues present in each chain of the seminal enzyme are involved in intersubunit bondsI documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.