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

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

doi:10.1159/000458828

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

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

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

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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 language	English (US)
Pages (from-to)	416-419
Number of pages	4
Journal	Enzyme
Volume	22
Issue number	6
DOIs	https://doi.org/10.1159/000458828
State	Published - Jan 1 1977

ASJC Scopus subject areas

Biochemistry

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

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.",

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N2 - 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.

AB - 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.

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

Abstract

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