THE PRIMARY STRUCTURE OF OVINE INTERSTITIAL CELL STIMULATING HORMONE IV: DISULFIDE BRIDGES OF THE β SUBUNIT
- 1 November 1975
- journal article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 7 (6) , 487-493
- https://doi.org/10.1111/j.1399-3011.1975.tb02470.x
Abstract
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.Keywords
This publication has 9 references indexed in Scilit:
- A simple procedure for separating the subunits of ovine and bovine pituitary interstitial cell stimulating hormoneArchives of Biochemistry and Biophysics, 1974
- The primary structure of ovine interstitial cell-stimulating hormoneArchives of Biochemistry and Biophysics, 1972
- The primary structure of ovine interstitial cell-stimulating hormoneArchives of Biochemistry and Biophysics, 1972
- The Primary Structure of Ovine Luteinizing HormonePublished by Elsevier ,1972
- The Primary Structure of Ovine Luteinizing HormoneJournal of Biological Chemistry, 1972
- Isolation and partial characterization of the polypeptide chains of ovine interstitial cell-stimulating hormoneBiochimica et Biophysica Acta (BBA) - Protein Structure, 1967
- Separation of dansyl-amino acids by polyamide layer chromatographyBiochimica et Biophysica Acta (BBA) - Protein Structure, 1967
- [52] Sequential degradation plus dansylationPublished by Elsevier ,1967
- Automatic Recording Apparatus for Use in Chromatography of Amino AcidsAnalytical Chemistry, 1958