Electrophoretic analysis of low and high activity forms of catechol-O-methyltransferase in human erythrocytes

Mark H. Grossman, Carol Szumlanski, James B. Littrell, Ronald Weinstein, Richard M Weinshilboum

Research output: Contribution to journalArticle

25 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)473-480
Number of pages8
JournalLife Sciences
Volume50
Issue number7
DOIs
StatePublished - 1992

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Catechol O-Methyltransferase
Thermodynamic stability
Hot Temperature
Erythrocytes
Genetic Techniques
Enzyme activity
Isoelectric Focusing
Enzymes
Electrophoresis
Sodium Dodecyl Sulfate
Molecular Biology
Polyacrylamide Gel Electrophoresis
Proteins

ASJC Scopus subject areas

  • Pharmacology

Cite this

Electrophoretic analysis of low and high activity forms of catechol-O-methyltransferase in human erythrocytes. / Grossman, Mark H.; Szumlanski, Carol; Littrell, James B.; Weinstein, Ronald; Weinshilboum, Richard M.

In: Life Sciences, Vol. 50, No. 7, 1992, p. 473-480.

Research output: Contribution to journalArticle

Grossman, Mark H. ; Szumlanski, Carol ; Littrell, James B. ; Weinstein, Ronald ; Weinshilboum, Richard M. / Electrophoretic analysis of low and high activity forms of catechol-O-methyltransferase in human erythrocytes. In: Life Sciences. 1992 ; Vol. 50, No. 7. pp. 473-480.
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