Detection of immunologically active zones in equine growth hormone
- 1 June 1976
- journal article
- research article
- Published by Wiley in European Journal of Immunology
- Vol. 6 (6), 409-417
- https://doi.org/10.1002/eji.1830060607
Abstract
Peptide fragments, obtained from equine growth hormone by cyanogen bromide cleavage and further chemical treatment, were isolated and identified. Their immunological reactivities were tested by hemagglutination and complement fixation methods using rabbit antisera against native hormone. Antigenic determinants were detected in the fragments comprising amino acid sequences 5–72 and 73–123, this last one being predominant. Fragment 124–178 had very low reactivity. Nitration of peptide 73–123 did not modify its immunological properties, but oxidation diminished them. Comparison of the antigenicity of equine growth hormone fragment 73–123 with that of the homologous ovine growth hormone fragment 86–123 lent support to the hypothesis that at least one antigenic determinant area in the horse hormone fragment is dependent on sequence 86–123.This publication has 24 references indexed in Scilit:
- Spontaneous Re-formation of a Broken Peptide ChainNature, 1974
- Studies on growth hormonesMolecular and Cellular Biochemistry, 1973
- The amino acid sequence of equine growth hormoneFEBS Letters, 1973
- Isolation, Purification and Characterization of Equine Growth HormoneEuropean Journal of Biochemistry, 1973
- Structural studies on ovine growth hormone Complete amino acid sequence, partially based on homology with bovine growth hormoneFEBS Letters, 1972
- AMINO ACID SEQUENCE OF SHEEP PITUITARY GROWTH HORMONEInternational Journal of Peptide and Protein Research, 1972
- Crosslinking during the nitration of bovine insulin with tetranitromethaneBiochemical and Biophysical Research Communications, 1970
- Isolation, Characterization and C-Terminal Sequence of Ovine Growth HormoneEuropean Journal of Biochemistry, 1970
- High recovery of tryptophan from acid hydrolysates of proteinsBiochemical and Biophysical Research Communications, 1969
- The Use of N-Bromosuccinimide and N-Bromoacetamide for the Selective Cleavage of C-Tryptophyl Peptide Bonds in Model Peptides and Glucagon1Journal of the American Chemical Society, 1960