Phenol plasma binding

Schmieder, PK. Henry, T.R. (1988) Plasma binding of 1-butanol, phenol, nitrobenzene and... 

Liao TF, Oehme FW. 1981. Tissue distribution and plasma protein binding of [14C] phenol in rats. Toxicol Appl Pharmacol 57 220-225. 

The affinity of polyphenols and various resveratrol analogs to compete for specific [3H]-resveratrol binding correlated very well (r = 0.74) with their neuroprotective activity against Ap25 35-induced toxicity in primary hippocampal cell cultures. This suggests that the neuroprotective effect exerted by these phenolic compounds could be mediated by a common mechanism involving specific polyphenol plasma membrane binding sites. 

Whether the occurrence of an enzyme in a particulate fraction really represents its in vivo location can be substantiated by the following properties (a) close binding to membrane lipids, cf. cyclopenase (D 8.4.2), which is a lipoprotein of the plasma membrane (b) cooperation with other enzymes, cf. the catalytic facilitation in the biosynthesis of cyanogenic glycosides, cinnamic and benzoic acids (A 3.1) and (c) in situ examination by cytochemical methods, cf. the localization of phenol oxidases (C 2.3.1), peroxidases (C 2.4) and thioglucosidases (D 9.4). 

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