Production of fetal-like alkaline phosphatase by HeLa cells

Norton A. Elson, Rody P. Cox

Research output: Contribution to journalArticle

52 Citations (Scopus)

Abstract

Alkaline phosphatase produced by HeLa cells differs in its chemical and physical properties from the enzyme found in adult organs and tissues (Cox and Griffin, 1967). In the present study HeLa cell alkaline phosphatase was compared to a fetal form of the enzyme found in human placenta. Both enzymes have approximately the same molecular weight as judged by sucrose density gradients, and the chemical and physical properties of these alkaline phosphatases are similar. The electrophoretic pattern of the HeLa cell enzyme resembles the placental alkaline phosphatase of the heterozygous FS phenotype except that it is slower moving. Double immunodiffusion using an antibody against HeLa cell alkaline phosphatase and placental and HeLa cell enzymes as antigens shows a single line of partial identity between the two enzymes, with a small spur suggesting additional antigenic sites on the HeLa cell enzyme. The data suggest that malignant cells in culture, HeLa, are producing a fetal-like alkaline phosphatase probably by "derepression of the genome." However, the electrophoretic and immunological characteristics of the enzyme are altered sufficiently so that it can be distinguished from the normally produced fetal enzyme.

Original languageEnglish (US)
Pages (from-to)549-561
Number of pages13
JournalBiochemical Genetics
Volume3
Issue number6
DOIs
StatePublished - Dec 1969

Fingerprint

HeLa Cells
phosphatase
Alkaline Phosphatase
alkaline phosphatase
enzyme
Enzymes
enzymes
cells
Chemical properties
chemical property
physical properties
physicochemical properties
Physical properties
physical property
Immunodiffusion
antigen
placenta
sucrose
Placenta
antibody

ASJC Scopus subject areas

  • Genetics
  • Biochemistry

Cite this

Production of fetal-like alkaline phosphatase by HeLa cells. / Elson, Norton A.; Cox, Rody P.

In: Biochemical Genetics, Vol. 3, No. 6, 12.1969, p. 549-561.

Research output: Contribution to journalArticle

@article{9cfc57183b94473d8cd8ad65339e4bed,
title = "Production of fetal-like alkaline phosphatase by HeLa cells",
abstract = "Alkaline phosphatase produced by HeLa cells differs in its chemical and physical properties from the enzyme found in adult organs and tissues (Cox and Griffin, 1967). In the present study HeLa cell alkaline phosphatase was compared to a fetal form of the enzyme found in human placenta. Both enzymes have approximately the same molecular weight as judged by sucrose density gradients, and the chemical and physical properties of these alkaline phosphatases are similar. The electrophoretic pattern of the HeLa cell enzyme resembles the placental alkaline phosphatase of the heterozygous FS phenotype except that it is slower moving. Double immunodiffusion using an antibody against HeLa cell alkaline phosphatase and placental and HeLa cell enzymes as antigens shows a single line of partial identity between the two enzymes, with a small spur suggesting additional antigenic sites on the HeLa cell enzyme. The data suggest that malignant cells in culture, HeLa, are producing a fetal-like alkaline phosphatase probably by {"}derepression of the genome.{"} However, the electrophoretic and immunological characteristics of the enzyme are altered sufficiently so that it can be distinguished from the normally produced fetal enzyme.",
author = "Elson, {Norton A.} and Cox, {Rody P.}",
year = "1969",
month = "12",
doi = "10.1007/BF00485476",
language = "English (US)",
volume = "3",
pages = "549--561",
journal = "Biochemical Genetics",
issn = "0006-2928",
publisher = "Springer New York",
number = "6",

}

TY - JOUR

T1 - Production of fetal-like alkaline phosphatase by HeLa cells

AU - Elson, Norton A.

AU - Cox, Rody P.

PY - 1969/12

Y1 - 1969/12

N2 - Alkaline phosphatase produced by HeLa cells differs in its chemical and physical properties from the enzyme found in adult organs and tissues (Cox and Griffin, 1967). In the present study HeLa cell alkaline phosphatase was compared to a fetal form of the enzyme found in human placenta. Both enzymes have approximately the same molecular weight as judged by sucrose density gradients, and the chemical and physical properties of these alkaline phosphatases are similar. The electrophoretic pattern of the HeLa cell enzyme resembles the placental alkaline phosphatase of the heterozygous FS phenotype except that it is slower moving. Double immunodiffusion using an antibody against HeLa cell alkaline phosphatase and placental and HeLa cell enzymes as antigens shows a single line of partial identity between the two enzymes, with a small spur suggesting additional antigenic sites on the HeLa cell enzyme. The data suggest that malignant cells in culture, HeLa, are producing a fetal-like alkaline phosphatase probably by "derepression of the genome." However, the electrophoretic and immunological characteristics of the enzyme are altered sufficiently so that it can be distinguished from the normally produced fetal enzyme.

AB - Alkaline phosphatase produced by HeLa cells differs in its chemical and physical properties from the enzyme found in adult organs and tissues (Cox and Griffin, 1967). In the present study HeLa cell alkaline phosphatase was compared to a fetal form of the enzyme found in human placenta. Both enzymes have approximately the same molecular weight as judged by sucrose density gradients, and the chemical and physical properties of these alkaline phosphatases are similar. The electrophoretic pattern of the HeLa cell enzyme resembles the placental alkaline phosphatase of the heterozygous FS phenotype except that it is slower moving. Double immunodiffusion using an antibody against HeLa cell alkaline phosphatase and placental and HeLa cell enzymes as antigens shows a single line of partial identity between the two enzymes, with a small spur suggesting additional antigenic sites on the HeLa cell enzyme. The data suggest that malignant cells in culture, HeLa, are producing a fetal-like alkaline phosphatase probably by "derepression of the genome." However, the electrophoretic and immunological characteristics of the enzyme are altered sufficiently so that it can be distinguished from the normally produced fetal enzyme.

UR - http://www.scopus.com/inward/record.url?scp=0014624029&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0014624029&partnerID=8YFLogxK

U2 - 10.1007/BF00485476

DO - 10.1007/BF00485476

M3 - Article

VL - 3

SP - 549

EP - 561

JO - Biochemical Genetics

JF - Biochemical Genetics

SN - 0006-2928

IS - 6

ER -