Optical activity of disulfide bonds in proteins. 1. Studies on plasmin modified human somatotropin

Biochemistry
T A Bewley

Abstract

The reduction and alkylation of the two disulfide bonds in a preparation of human pituitary growth hormone which had been previously modified by limited proteolysis with the enzyme plasmin have been studied. Quantitative and selective reduction of the carboxyl-terminal disulfide, as well as total reduction of both disulfides, has been achieved in the absence of denaturants. Circular dichroism spectra of the various reduced and reduced-alkylated derivatives have provided sufficient information to allow an estimation of the individual contributions of each disulfide bond to the total optical activity of the protein. These contributions were found to represent a significant portion of the total optical activity between 290 and 250 nm. The carboxyl-termimal bond exhibits negative dichroism with an apparent center near 258 nm ([theta]M,258nm = 2100 deg cm2 dmol-1). By comparison, the contribution of the remaining disulfide is red-shifted to 273 nm, is also negative in sign, and somewhat more intense ([theta]M,273nm = 3200 deg cm2 dmol-1). Circular dichroism measurements have also been used to approximate the rate of reduction of the protein.

References

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Citations

Sep 1, 1983·Archives of Biochemistry and Biophysics·T A BewleyF Talamantes
Jun 6, 2009·Journal of Cellular Biochemistry·Xuerong ShiRichard K Gordon
Apr 1, 1983·International Journal of Peptide and Protein Research·J M DelfinoJ A Santomé
Mar 1, 1982·International Journal of Peptide and Protein Research·M SogamiH Inouye
Nov 1, 1978·International Journal of Peptide and Protein Research·T A Bewley, Y Birk
Mar 17, 2021·Biological Trace Element Research·Sergey A MiroshnikovAlexey A Tinkov

Related Concepts

Alkylation
Circular Dichroism, Vibrational
Disulfides
Sputolysin
Fibrogammin
Oxidation-Reduction
Polypeptides
Recombinant Growth Hormone

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