Abstract
Changes in the configuration of proteins were studied by the modifications of the ultraviolet absorption of their alkaline solutions. These were expressed in terms of the ratio O.D. pH12/O.D. pH7, termed side-group ionization ratio (SGIR). This ratio showed two peaks; one at 300 to 305 mµ is known to correspond to the phenolic hydroxyl of tyrosine and another at 245 mµ seems to be caused by the ionization of the sulfhydryl group of cysteine. The SGIR of extracts from electrically stimulated nerve structures was found to be consistently and significantly higher than that of similar extracts from resting tissues. The phenomenon was observed in isolated nerves (frog and rat sciatic) stimulated in vitro and in the cerebral cortex of cats, dogs, and rats after stimulation of their afferents. The increase in SGIR was reversible if the stimulated structures were allowed to rest. Prolonged stimulation, in addition to causing structural changes, also caused breakdown of proteins and the appearance of proteolytic activity. The latter, studied on a synthetic substrate, could be detected even after shorter stimuli, together with configurational changes but without proteolysis. The structural changes detected with the spectrophotometric method are closely related to reversible denaturation as produced by urea. The changes probably involve rupture of hydrogen bonds which loosens the protein molecule and perhaps changes its affinity for different ions. It is possible that such a process may play a role in the mechanism of excitation.
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Selected References
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- Crammer J. L., Neuberger A. The state of tyrosine in egg albumin and in insulin as determined by spectrophotometric titration. Biochem J. 1943 Jul;37(2):302–310. doi: 10.1042/bj0370302. [DOI] [PMC free article] [PubMed] [Google Scholar]
- FOLCH J., LEES M. Proteolipides, a new type of tissue lipoproteins; their isolation from brain. J Biol Chem. 1951 Aug;191(2):807–817. [PubMed] [Google Scholar]
- STEINHARDT J., ZAISER E. M. Hydrogen ion equilibria in native and denatured proteins. Adv Protein Chem. 1955;10:151–226. doi: 10.1016/s0065-3233(08)60105-9. [DOI] [PubMed] [Google Scholar]
- WALD G., BROWN P. K. The role of sulfhydryl groups in the bleaching and synthesis of rhodopsin. J Gen Physiol. 1952 May;35(5):797–821. doi: 10.1085/jgp.35.5.797. [DOI] [PMC free article] [PubMed] [Google Scholar]