Immunological characterization of oncofetal alkaline phosphatases from human placenta and HeLa71 cells

N. K. Ghosh, R. P. Cox

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Human placental alkaline phosphatase (AP) exhibits a genetic polymorphism that is determined by the genotype of the fetus. A similar enzyme is produced by certain neoplasms and by some cells in culture. The relations between these enzymes were investigated by immunologic methods comparing human placental AP to the AP of HeLa71 cells. Antiserum prepared against placental AP precipitated 90% of the enzyme and the catalytic activity was quantitatively recovered in the antigen antibody precipitate. Enzyme antibody complexes failed to migrate on starch gel electrophoresis. Antiserum against placental AP cross reacted with HeLa71 AP and HeLa71 AP antiserum reacted with the placental enzyme. Immunologic analysis by double diffusion in agar showed that the 3 common genetic variants of placental AP - F, FS and S - and HeLa71 AP were closely related when studied by antisera against both placental or HeLa71 AP. When studied by immunodiffusion the genetic variants of human placental AP and the HeLa enzyme reacted with identity at the points of contact of the precipitation lines when precipitated by antisera against either enzyme. These findings support the view that the human placental and HeLa71 APs are products of the same genetic locus. Derepression of a portion of the genome in association with malignant transformation might be responsible for ectopic production of this enzyme in HeLa71 cells.

Original languageEnglish (US)
Pages (from-to)35-45
Number of pages11
JournalENZYME
Volume20
Issue number1
StatePublished - 1975

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Placenta
Alkaline Phosphatase
Immune Sera
Enzymes
Starch Gel Electrophoresis
Genetic Loci
Antibodies
Immunodiffusion
Medical Genetics
Genetic Polymorphisms
Electrophoresis
Polymorphism
Starch
Agar
placental alkaline phosphatase
Precipitates
Catalyst activity
Fetus
Cell Culture Techniques
Genes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Immunological characterization of oncofetal alkaline phosphatases from human placenta and HeLa71 cells. / Ghosh, N. K.; Cox, R. P.

In: ENZYME, Vol. 20, No. 1, 1975, p. 35-45.

Research output: Contribution to journalArticle

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abstract = "Human placental alkaline phosphatase (AP) exhibits a genetic polymorphism that is determined by the genotype of the fetus. A similar enzyme is produced by certain neoplasms and by some cells in culture. The relations between these enzymes were investigated by immunologic methods comparing human placental AP to the AP of HeLa71 cells. Antiserum prepared against placental AP precipitated 90{\%} of the enzyme and the catalytic activity was quantitatively recovered in the antigen antibody precipitate. Enzyme antibody complexes failed to migrate on starch gel electrophoresis. Antiserum against placental AP cross reacted with HeLa71 AP and HeLa71 AP antiserum reacted with the placental enzyme. Immunologic analysis by double diffusion in agar showed that the 3 common genetic variants of placental AP - F, FS and S - and HeLa71 AP were closely related when studied by antisera against both placental or HeLa71 AP. When studied by immunodiffusion the genetic variants of human placental AP and the HeLa enzyme reacted with identity at the points of contact of the precipitation lines when precipitated by antisera against either enzyme. These findings support the view that the human placental and HeLa71 APs are products of the same genetic locus. Derepression of a portion of the genome in association with malignant transformation might be responsible for ectopic production of this enzyme in HeLa71 cells.",
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AB - Human placental alkaline phosphatase (AP) exhibits a genetic polymorphism that is determined by the genotype of the fetus. A similar enzyme is produced by certain neoplasms and by some cells in culture. The relations between these enzymes were investigated by immunologic methods comparing human placental AP to the AP of HeLa71 cells. Antiserum prepared against placental AP precipitated 90% of the enzyme and the catalytic activity was quantitatively recovered in the antigen antibody precipitate. Enzyme antibody complexes failed to migrate on starch gel electrophoresis. Antiserum against placental AP cross reacted with HeLa71 AP and HeLa71 AP antiserum reacted with the placental enzyme. Immunologic analysis by double diffusion in agar showed that the 3 common genetic variants of placental AP - F, FS and S - and HeLa71 AP were closely related when studied by antisera against both placental or HeLa71 AP. When studied by immunodiffusion the genetic variants of human placental AP and the HeLa enzyme reacted with identity at the points of contact of the precipitation lines when precipitated by antisera against either enzyme. These findings support the view that the human placental and HeLa71 APs are products of the same genetic locus. Derepression of a portion of the genome in association with malignant transformation might be responsible for ectopic production of this enzyme in HeLa71 cells.

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