Open AccessTHIOLATION OF PROTEINS
Author(s) -
Reinhold Benesch,
Ruth E. Benesch
Publication year - 1958
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.44.9.848
Subject(s) - induced pluripotent stem cell , drug discovery , myocyte , in vitro , microbiology and biotechnology , stem cell , computational biology , cardiac electrophysiology , cardiac cell , cell , cardiac muscle , biology , fluorescence microscope , neuroscience , electrophysiology , bioinformatics , anatomy , biochemistry , fluorescence , embryonic stem cell , physics , quantum mechanics , gene
The application of this reaction to the thiolation of proteins was limited by the fact that a relatively high pH and long reaction times were required to obtain good yields. We have now found that in the presence of silver the thiolation proceeds rapidly at room temperature in aqueous solution at pH 7.5. A similar effect of silver on the aminolysis of certain thiolesters has been reported by Schwyzer.2 Somewhat unexpectedly, silver and AHTL react to form an insoluble complex. A maximum of 2 Ag+ per mole of AHTL is bound and one proton is liberated for each equivalent of silver. It is the insoluble silver complex which reacts with protein amino groups.
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