Activity of aspartate transcarbamylase in uninfected and type 5 adenovirus-infected HeLa cells.

Journal of bacteriology ·Vol. 87 ·No. 5 ·1964-05-00 ·Pages 1034-43

Consigli RA, Ginsberg HS

Abstract

Consigli, Richard A. (University of Pennsylvania, Philadelphia), and Harold S. Ginsberg. Activity of aspartate transcarbamylase in uninfected and type 5 adenovirus-infected HeLa cells. J. Bacteriol. 87:1034-1043. 1964.-A two- to three-fold increase in aspartate transcarbamylase (ATCase) activity was observed in type 5 adenovirus-infected HeLa cells 18 hr after infection. The enhanced enzyme activity was virus-specific and dependent on biosynthesis of deoxyribonucleic acid and protein. When various characteristics as well as the kinetics of the enzymes from uninfected and infected cells were compared, ATCase from adenovirus-infected cells was shown to have an altered pH optimum, greater heat stability, increased maximal velocity, and increased K(m) value for aspartate.

MeSH Terms

Adenoviridae/enzymology Chromatography Culture Techniques DNA/biosynthesis Floxuridine/pharmacology HeLa Cells Hot Temperature Hydrogen-Ion Concentration Kinetics Toxins, Biological Transferases/metabolism

Chemicals

Toxins, Biological Floxuridine DNA Transferases

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Consigli R A

Ginsberg H S

References (27)

27 references, click to expand

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Article Info

Journal

Journal of bacteriology

Abbr.

J Bacteriol

ISSN

0021-9193

DOI

10.1128/jb.87.5.1034-1043.1964

Published

1964-05-00

Pages

1034-43

Language

English

Region

United States

NLM ID

2985120R

PMCID

PMC277142

Subset

External Links

PubMed source DOI: 10.1128/jb.87.5.1034-1043.1964 PMC Full Text View journal details

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Activity of aspartate transcarbamylase in uninfected and type 5 adenovirus-infected HeLa cells.

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