Bioautographic visualization of dihydrofolate reductase in enzyme overproducing BHK mutants

S. L. Naylor; J. K. Townsend; R. J. Klebe

doi:10.1007/BF00504369

Bioautographic visualization of dihydrofolate reductase in enzyme overproducing BHK mutants

S. L. Naylor, J. K. Townsend, R. J. Klebe

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

1 Scopus citations

Abstract

A bioautographic procedure has been developed for the visualization of the isozymes of dihydrofolate reductase (DHFR, E.C. 1.5.1.3). In addition to detecting electrophoretically separated enzymes, bioautography was utilized to visualize DHFR after isoelectric focusing on polyacrylamide gels. Both zone electrophoresis and isoelectric focusing were used to compare wildtype BHK cells to mutants which overproduce dihydrofolate reductase. In agreement with other physical data, the BHK-A5 overproduction mutant appears to produce more dihydrofolate reductase of the same electrophoretic mobility and isoelectric point as wild type cells.

Original language	English (US)
Pages (from-to)	199-206
Number of pages	8
Journal	Biochemical Genetics
Volume	18
Issue number	1-2
DOIs	https://doi.org/10.1007/BF00504369
State	Published - Feb 1980
Externally published	Yes

Keywords

bioautography
dihydrofolate reductase
electrophoresis
mutant cells

ASJC Scopus subject areas

Ecology, Evolution, Behavior and Systematics
Biochemistry
Molecular Biology
Genetics

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10.1007/BF00504369

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title = "Bioautographic visualization of dihydrofolate reductase in enzyme overproducing BHK mutants",

abstract = "A bioautographic procedure has been developed for the visualization of the isozymes of dihydrofolate reductase (DHFR, E.C. 1.5.1.3). In addition to detecting electrophoretically separated enzymes, bioautography was utilized to visualize DHFR after isoelectric focusing on polyacrylamide gels. Both zone electrophoresis and isoelectric focusing were used to compare wildtype BHK cells to mutants which overproduce dihydrofolate reductase. In agreement with other physical data, the BHK-A5 overproduction mutant appears to produce more dihydrofolate reductase of the same electrophoretic mobility and isoelectric point as wild type cells.",

keywords = "bioautography, dihydrofolate reductase, electrophoresis, mutant cells",

author = "Naylor, {S. L.} and Townsend, {J. K.} and Klebe, {R. J.}",

year = "1980",

month = feb,

doi = "10.1007/BF00504369",

language = "English (US)",

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pages = "199--206",

journal = "Biochemical Genetics",

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AU - Naylor, S. L.

AU - Townsend, J. K.

AU - Klebe, R. J.

PY - 1980/2

Y1 - 1980/2

N2 - A bioautographic procedure has been developed for the visualization of the isozymes of dihydrofolate reductase (DHFR, E.C. 1.5.1.3). In addition to detecting electrophoretically separated enzymes, bioautography was utilized to visualize DHFR after isoelectric focusing on polyacrylamide gels. Both zone electrophoresis and isoelectric focusing were used to compare wildtype BHK cells to mutants which overproduce dihydrofolate reductase. In agreement with other physical data, the BHK-A5 overproduction mutant appears to produce more dihydrofolate reductase of the same electrophoretic mobility and isoelectric point as wild type cells.

AB - A bioautographic procedure has been developed for the visualization of the isozymes of dihydrofolate reductase (DHFR, E.C. 1.5.1.3). In addition to detecting electrophoretically separated enzymes, bioautography was utilized to visualize DHFR after isoelectric focusing on polyacrylamide gels. Both zone electrophoresis and isoelectric focusing were used to compare wildtype BHK cells to mutants which overproduce dihydrofolate reductase. In agreement with other physical data, the BHK-A5 overproduction mutant appears to produce more dihydrofolate reductase of the same electrophoretic mobility and isoelectric point as wild type cells.

KW - bioautography

KW - dihydrofolate reductase

KW - electrophoresis

KW - mutant cells

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Bioautographic visualization of dihydrofolate reductase in enzyme overproducing BHK mutants

Abstract

Keywords

ASJC Scopus subject areas

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