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Isoelectric point, glutathione

Thiol methyltransferase has been detected in erythrocytes, lymphocytes, lungs, cecal, and colonic mucosae. The nature and number of thiol methyltransferases is not clear at the present time. A cytosolic enzyme and a microsomal enzyme have been reported, with the microsomal enzyme being dissociated from membrane relatively easily. The microsomal enzyme in rat liver has been purified to homogeneity. The enzyme is a 28,000-dalton monomer with an isoelectric point of 6.2. A wide variety of xenobiotic thiols are methylated, but cysteine and glutathione are not substrates. S-Methylation is an important component in the thiomethyl shunt. Thiomethyl conjugates are metabolized to the methylsulfoxides by oxidation (see Chapter 10) and reenter the mercapturic acid pathway as substrates for glutathione S-transferase. [Pg.228]


See other pages where Isoelectric point, glutathione is mentioned: [Pg.254]    [Pg.76]    [Pg.178]    [Pg.304]    [Pg.311]    [Pg.392]    [Pg.146]    [Pg.160]    [Pg.12]    [Pg.81]    [Pg.194]   
See also in sourсe #XX -- [ Pg.48 ]




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