title: Electrophoretic analysis of low and high activity forms of catechol-O-methyltransferase in human erythrocytes.
abstract: Analysis of the catechol-O-methyltransferase (COMT) enzyme in human RBC lysates from 15 samples exhibiting inherited variations in level of activity and thermal stability was performed. Electrophoretic blotting and immune fixation was carried out following sodium dodecyl sulfate polyacrylamide gel electrophoresis or isoelectric focusing of lysate protein. These techniques did not reveal a major structural alteration of the protein that could account for the observed variation in enzyme activity or thermal stability. Future studies utilizing molecular genetic techniques should make it possible to determine the basis for inherited variations in human RBC COMT activity and thermal stability.
authors.affiliation: Department of Pediatrics, Temple University School of Medicine, St. Christopher's Hospital for Children, Philadelpiha, PA 19134.
authors.forename: M H
authors.initials: MH
authors.lastname: Grossman
authors.forename: C
authors.initials: C
authors.lastname: Szumlanski
authors.forename: J B
authors.initials: JB
authors.lastname: Littrell
authors.forename: R
authors.initials: R
authors.lastname: Weinstein
authors.forename: R M
authors.initials: RM
authors.lastname: Weinshilboum
mesh_terms: D002394:Catechol O-Methyltransferase / Q000097:blood* / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D015151:Immunoblotting; D007526:Isoelectric Point; D008970:Molecular Weight; D010641:Phenotype; D011110:Polymorphism, Genetic; D011897:Random Allocation; D013329:Structure-Activity Relationship
chemical_list: D002394:Catechol O-Methyltransferase