Abstract：
:We have determined that the addition of 3-phenylamino-L-alanine (PAA), a recently reported contaminant in L-tryptophan implicated in the eosinophilia-myalgia syndrome, affects tryptophan binding by utilizing an in vitro measurement of 3H-tryptophan binding to hepatic nuclei or nuclear envelopes. PAA (10(-10) to 10(-4) M) diminishes the inhibitory effect of binding due to excess unlabeled L-tryptophan (10(-4) M). PAA alone has no inhibitory effect on binding. The effect of PAA on in vitro tryptophan binding is in contrast to that of another contaminant, 1,1'-ethylidenebis(tryptophan), which together with excess unlabeled L-tryptophan does not appreciably affect the binding. In vitro addition of PAA and L-tryptophan to nuclei of rat brain or of cultured murine macrophages does not affect [3H]tryptophan binding in comparison to L-tryptophan alone as is the case with hepatic nuclear envelopes. Adding PAA to an in vitro protein synthesis system and measuring [3H]tryptophan or [3H]alanine incorporation into acid-precipitable proteins reveals that it competes similarly, but somewhat less, than does equimolar concentrations of unlabeled L-tryptophan or L-alanine, respectively. This suggests that PAA or a breakdown compound becomes incorporated into proteins. Speculation as to how PAA may affect tissues in experimental animals is presented.
journal_name
Toxicologyjournal_title
Toxicologyauthors
Sidransky H,Verney E,Cosgrove JW,Latham PSdoi
10.1016/0300-483x(94)90058-2subject
Has Abstractpub_date
1994-01-26 00:00:00pages
135-45issue
1-2eissn
0300-483Xissn
1879-3185pii
0300-483X(94)90058-2journal_volume
86pub_type
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