| Literature DB >> 6109281 |
D E Sok, J K Pai, V Atrache, C J Sih.
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.Entities:
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Year: 1980 PMID: 6109281 PMCID: PMC350309 DOI: 10.1073/pnas.77.11.6481
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205