Results 271 to 280 of about 166,609 (297)
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Reversible inactivation and superactivation by covalent modification of thermolysin
Biochemical and Biophysical Research Communications, 1973Abstract Diethylpyrocarbonate (DEP) in the pH range 6.1 – 7.5 inactivates thermolysin by ethoxyformylation. Restoration of activity by hydroxylamine at pH 6.2 correlates with the regeneration of a single histidyl residue. Exposure of the enzyme to DEP together with the reversible inhibitor β-phenylpropionyl-L-phenylalanine, or acylation with the ...
S, Blumberg, B, Holmquist, B L, Vallee
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Improvement by Covalent and Noncovalent Modification
1978As mentioned in earlier Chapters, cyclodextrins exhibit many interesting features such as rate effects, stereospecificity, enantiomeric specificity, etc., in organic reactions. However, there is one serious hortcoming of cyclodextrins as catalysts.
Myron L. Bender, Makoto Komiyama
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Tyrosinase enhances the covalent modification of DNA by dopamine
Molecular Brain Research, 1996Dopamine-induced DNA damage was studied in vitro in the presence of the enzyme tyrosinase. Dopamine auto-oxidizes to form dopamine quinone, a reactive molecule which spontaneously decomposes to form additional reactive species that can modify cellular macromolecules.
A H, Stokes +4 more
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Posttranslational covalent modification of proteins.
Science (New York, N.Y.), 1978A search for derivatized amino acids in proteins has shown that the extent of posttranslational modification of proteins is quite substantial. While only 20 primary amino acids are specified in the genetic code and are involved as monomer building blocks in the assembly of the polypeptide chain, about 140 amino acids and amino acid derivatives have ...
R, Uy, F, Wold
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Covalent modification of nuclear proteins during aging
1975An in vitro assay system has been established to study acetylation and phosphorylation of nuclear proteins from isolated nuclei. Phosphorylation of neclear proteins reached a peak within 5 min while maximum acetylation occurred about 10 min later. The rate of acetylation of liver nuclear proteins in 15 min incubation was significantly higher in "old ...
Liew, C C, Gornall, A G
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Nonenzymatic Covalent Posttranslational Modification of Proteins In Vivo
1985Publisher Summary This chapter presents the in vivo analysis of non-enzymatic covalent post-translational modification of proteins. Enzyme-controlled post-translational modification of proteins, especially enzymes, has been demonstrated in many tissues and organisms. These post-translational modifications are of the utmost importance in the control
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Sequence selectivity of DNA covalent modification
Chemical Research in Toxicology, 1988M A, Warpehoski, L H, Hurley
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