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

doi:10.1016/0024-3205(92)90386-4

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

Pharmacology

Research output: Contribution to journal › Article › peer-review

25 Scopus citations

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 language	English (US)
Pages (from-to)	473-480
Number of pages	8
Journal	Life Sciences
Volume	50
Issue number	7
DOIs	https://doi.org/10.1016/0024-3205(92)90386-4
State	Published - 1992

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)
Pharmacology, Toxicology and Pharmaceutics(all)

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10.1016/0024-3205(92)90386-4

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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.",

author = "Grossman, {Mark H.} and Carol Szumlanski and Littrell, {James B.} and Ronald Weinstein and Weinshilboum, {Richard M.}",

note = "Funding Information: This work was supported by grants from the NIH \[NS 24066 (M.H.G.), GM 38157 and GM 35720 (R.M.W.)\] and the Scottish Rite Schizophrenia Research Program, N.M.J., USA (M.H.G.), and by NIEHS contract ES 05304 (R.M.W.).",

year = "1992",

doi = "10.1016/0024-3205(92)90386-4",

language = "English (US)",

volume = "50",

pages = "473--480",

journal = "Life Sciences",

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T1 - Electrophoretic analysis of low and high activity forms of catechol-O-methyltransferase in human erythrocytes

AU - Grossman, Mark H.

AU - Szumlanski, Carol

AU - Littrell, James B.

AU - Weinstein, Ronald

AU - Weinshilboum, Richard M.

N1 - Funding Information: This work was supported by grants from the NIH \[NS 24066 (M.H.G.), GM 38157 and GM 35720 (R.M.W.)\] and the Scottish Rite Schizophrenia Research Program, N.M.J., USA (M.H.G.), and by NIEHS contract ES 05304 (R.M.W.).

PY - 1992

Y1 - 1992

N2 - 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.

AB - 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.

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JO - Life Sciences

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

Abstract

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