A vibrational spectroscopic assignment of the disulfide bridges in recombinant bovine growth hormone and growth hormone analogs.
Disulfide stretching vibrations for bovine growth hormone (bGH) occur in a vibrational envelope centered at 540 cm-1 which spans 480-580 cm-1. A multitude of vibrational bands present in this envelope, that are not related to disulfide stretching, emphasize the need for model compounds when assigning S-S stretching modes. Raman spectroscopic data for bGH analogs, in which one or both of the two disulfide bridges have been selectively cleaved, have been used to characterize the S-S stretching envelope for the two cystine links in bGH. The Raman data for the r-bGH analogs indicate that the number of disulfide bonds present in r-bGH is determined, not by the observance of the presence or absence of a single spectral peak, but by the relative intensity of vibrational envelope from 520-560 cm-1. Cleavage of disulfide bridges in bGH results in a general decrease in vibrational spectral intensity in the 520-560 cm-1 range. This decrease in intensity is proportional to the number of cystine links severed.
Thamann
T J
TJ
Upjohn, Inc., Kalamazoo, MI 49001, USA. thomas.j.thamann@am.pnu.com
D000818:Animals; D002417:Cattle; D004220:Disulfides / Q000737:chemistry; D013006:Growth Hormone / Q000031:analogs & derivatives* / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D013059:Spectrum Analysis, Raman / Q000379:methods*
D004220:Disulfides; D011994:Recombinant Proteins; D013006:Growth Hormone