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Cysteine chemical modification reagents

Chemical modification reagents for labelling reactive amino acid side chains (predominantly cysteine or lysine) have been available for many years and used to probe for residues dose to or in the active site of enzymes. Although fluorescent derivative,s of these reagents have been used less frequently, they occasionally reward persistent experimentation by offering more detailed... [Pg.260]

Two of the cysteine residues are especially reactive toward chemical modification. Thus, one residue per subunit is selectively alkylated with iodoacetate (55) and a different one with butylisocyanate 406,407). In both cases the enzyme is inactivated and protected by the coenzyme against modification, suggesting that these residues are at the active sites of the enzyme. The two residues are now known 12,137) to be homologous to the two reactive cysteine residues in the horse enzyme, Cys-46 and Cys-174 (Section II,E,l,a), which are ligands to the active site zinc atom (Section II,C,3,b). A number of other reagents, apart from reactive coenzyme analogs, have also been shown to modify essential cysteine residues, i.e., probably either of these residues. Thus, one cysteine residue... [Pg.176]

Methyl p-Nitrobenzenesulfonate, p-Nitrobenzene-sulfonic acid methyl ester. C,HTNO,S mol wt 217.20. C 38.71%, H 3.25%, N 6.45%, O 36.83%, S 14.76%. Reagent for selective methylation or cysteine residues in chemical modification of proteins Nakagawa, Bender, J. dm. Chem. Sac, 91, 1566(1969). Procedure Heinrikson. Biochem. Bio-phys. Res. Common. 41, 967 (1970). Prepd by the general method of reacting p-nitrobenzenesulfony] chloride with alcohols. See Morgan, Cretcher, J. Am. Chem Soc. 70, 375 (1948). [Pg.959]

In the bovine heart mitochondrial ADP/ATP carrier, there are four cysteine residues Cys , Cys , Cys and Cys which are all at intervals of about 100 amino acid residues except Cys . This paper deals with the molecular mechanism of substrate transport by the carrier, deduced mainly from the effects of chemical modifications of its cysteine residues by SH-reagents under various conditions. The important role of the loops of the carrier in its transport function is described. Unless otherwise noted, the results were obtained with bovine heart submito-chondrial particles, in which the orientation of membrane proteins is inside-out relative to that of mitochondria. [Pg.204]


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See also in sourсe #XX -- [ Pg.755 ]

See also in sourсe #XX -- [ Pg.755 ]




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