thiol

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thiol

 [thi´ol]
2. any organic compound containing the —SH group bound to carbon.

thi·ol

(thī'ol),
1. The monovalent radical -SH when attached to carbon; a hydrosulfide; a mercaptan.
2. A mixture of sulfurated and sulfonated petroleum oils purified with ammonia; used in the treatment of skin diseases.

thiol

/thi·ol/ (thi´ol)
2. any organic compound containing the —SH group.

thi·ol

(thī'ol)
Mixture of sulfurated and sulfonated petroleum oils purified with ammonia; used to treat skin diseases.
References in periodicals archive ?
Lead thiolate containing precursor gels were prepared using conventional sol-gel processing techniques (Brinker and Scherer, 1990).
The gel was dried at 125[degrees]C for 30 min affording a dry, pale yellow lead thiolate doped silica gel precursor.
In this study, the accelerator thiolate fragment is considered directly coordinated to the zinc ion, not through a `poly-sulfur' or `poly-sulfur-thiolate' chain.
Hence, accelerator thiolate complexes having lower electron density in the S-Zn bond, higher electron density in the C-N bond and a weaker interaction between the ligand N and Zn, favor an increased rate of reaction.
Metal thiolates were separated by vacuum filtration and washed several times by acetone, then they were purified by dissolution in hot chloroform (50[degrees]C) and reprecipitated by ethanol addition.
Albumin thiolate anion is an intermediate in the formation of album in-S-S-homocysteine.
Data show that the sulfhydryl thiolate state is a significantly softer ([sigma]) nucleophile than either the corresponding thiol state or the other amino acid residues such as histidine or lysine.
1990), their ability to bind heavy metals, as with the MT1A isoform, depends on several factors: MT abundance in target tissues, mercury form in target tissues, and redox chemistry of MT and thiolate (Maret and Vallee 1998).
Gut microbes were found to thiolate and methvlate arsenic in both human and mouse models (Pinyayev et al.
2]-mediated inactivation of protein thiols is found in redox regulation of protein tyrosine phosphatases, in which the cysteine thiolate in the catalytic center of the enzyme is reversibly oxidized by [H.
CYTOCHROME P-450 SUPERFAMILY OF HEME THIOLATE PROTEINS
Forty-four of those electrons were immobilized in bonds between gold atoms and thiolates, leaving 58 electrons to fill a shell around the "superatom.