Comparison of aldolase isozymes in placenta, HeLa cells, and human fibroblast cultures

R. Gliksman, N. K. Ghosh, R. P. Cox

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

The aldolase specific activity of the human carcinoma cell line, HeLa, against fructose 1,6-diphosphate as substrate is 4- to 5-fold greater than the specific activity of diploid human fibroblast cultures derived from skin and lung. HeLa aldolase isozyme is predominantly the A type and its substrate preferences resemble human placenta. These findings provide further support for the oncofetal enzyme constitution of HeLa cells.

Original languageEnglish (US)
Pages (from-to)416-419
Number of pages4
JournalENZYME
Volume22
Issue number6
StatePublished - 1977

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Fructose-Bisphosphate Aldolase
Fibroblasts
HeLa Cells
Cell culture
Human Activities
Placenta
Isoenzymes
Constitution and Bylaws
Substrates
Diploidy
Skin
Cells
Carcinoma
Cell Line
Lung
Enzymes
fructose-1,6-diphosphate

ASJC Scopus subject areas

  • Biochemistry

Cite this

Comparison of aldolase isozymes in placenta, HeLa cells, and human fibroblast cultures. / Gliksman, R.; Ghosh, N. K.; Cox, R. P.

In: ENZYME, Vol. 22, No. 6, 1977, p. 416-419.

Research output: Contribution to journalArticle

Gliksman, R. ; Ghosh, N. K. ; Cox, R. P. / Comparison of aldolase isozymes in placenta, HeLa cells, and human fibroblast cultures. In: ENZYME. 1977 ; Vol. 22, No. 6. pp. 416-419.
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