Vibrational spectroscopic studies of solid recombinant bovine growth hormone and related growth hormone analogs.
Infrared and Raman spectra have been obtained for lyophilized recombinant bovine growth hormone (r-bGH), partially reduced, and completely reduced r-bGH, plus a tryptic digest fragment of r-bGH. Amide I and II data indicate r-bGH to have substantial helical character. Partially reduced r-bGH, in which the carboxyl terminal disulfide bridge (residues 181, 189) has been cleaved, has slightly less helical content than r-bGH. The spectral data indicate that breaking the carboxyl terminal cystine link produces only localized structural alterations. The additional cleavage of the second disulfide bridge (residues 53,164) leads to a further decrease in helix content, accompanied by increases in beta-sheet and disordered structures. A tryptic digest r-bGH fragment (residues 96-133), which contains a small amount of biological activity (approximately 10%), has predominantly helical structure.
Thamann
T J
TJ
Upjohn, Inc., Kalamazoo, MI 49001, USA. thomas.j.thamann@am.pnu.com
Chao
R S
RS
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D004220:Disulfides; D013006:Growth Hormone / Q000737:chemistry*; D006728:Hormones / Q000737:chemistry*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D017433:Protein Structure, Secondary; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods; D013059:Spectrum Analysis, Raman / Q000379:methods; D014357:Trypsin
D004220:Disulfides; D006728:Hormones; D010446:Peptide Fragments; D011993:Recombinant Fusion Proteins; D013006:Growth Hormone; D014357:Trypsin