The primary structure of ovine interstitial cell stimulating hormone. IV: Disulfide bridges of the beta subunit.
The disulfide linkage of the 12 half-cystine residues in the beta subunit of ovine interstitial cell stimulating hormone has been investigated by enzymic and partial acid hydrolysis of the intact molecule. Results indicate that the disulfide bridges are formed by residues 9-38, 23-72, 26-110, 34-90, 57-88, and 93-100.
D000595:Amino Acid Sequence; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D003553:Cystine; D006868:Hydrolysis; D007986:Luteinizing Hormone / Q000032:analysis; D010446:Peptide Fragments / Q000032:analysis; D011485:Protein Binding; D011487:Protein Conformation; D012756:Sheep
D010446:Peptide Fragments; D003553:Cystine; D007986:Luteinizing Hormone