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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1980 Nov;77(11):6481–6485. doi: 10.1073/pnas.77.11.6481

Characterization of slow reacting substances (SRSs) of rat basophilic leukemia (RBL-1) cells: effect of cysteine on SRS profile.

D E Sok, J K Pai, V Atrache, C J Sih
PMCID: PMC350309  PMID: 6109281

Abstract

When RBL-1 cells were incubated with L-cysteine (7.5 mM) and the ionophore A23187, the slow reacting substances SRS-GSH and SRS-Cys-Gly were formed. When L-cysteine was omitted in the incubation, SRS-GSH and SRS-Cys were isolated but only a trace amount of SRS-Cys-Gly was detectable. Each of the characterized SRSs was accompanied by an as yet uncharacterized structural isomer showing UV absorption at 278 nm. L-Cysteine and other thiols inhibited an aminopeptidase that transforms the highly bioactive SRS of anaphylaxis (SRS-Cys-Gly) into the less bioactive SRS-Cys. SRS-GSH, SRS-Cys-Gly, and SRS-Cys may be readily distinguished from each other by means of their bioactivities, antagonism by FPL 55712, and relative susceptibilities to the actions of soybean lipoxygenase, microsome-bound leucine aminopeptidase, and gamma-glutamyl transpeptidase.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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