Detection of enzyme polymorphism by using monoclonal antibodies

C. A. Slaughter; M. C. Coseo; M. P. Cancro; H. Harris

doi:10.1073/pnas.78.2.1124

Detection of enzyme polymorphism by using monoclonal antibodies

C. A. Slaughter, M. C. Coseo, M. P. Cancro, H. Harris

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Abstract

Six monoclonal antibodies against human placental alkaline phosphatase [orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1], a highly polymorphic enzyme, were tested for reactivity against a panel of 295 placental extracts that had been typed electrophoretically. The products of the three common alleles as well as several rare alleles could be discriminated by the various antibodies. In some cases differences between allelic products were reflected by essentially 'all-or-none' reactions, but in other cases the differences were smaller and demonstrable only by quantitative analysis of the binding. Evidence for allelic differences not detectable electrophoretically was also obtained.

Original language	English (US)
Pages (from-to)	1124-1128
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	78
Issue number	2 II
DOIs	https://doi.org/10.1073/pnas.78.2.1124
State	Published - 1981
Externally published	Yes

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title = "Detection of enzyme polymorphism by using monoclonal antibodies",

abstract = "Six monoclonal antibodies against human placental alkaline phosphatase [orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1], a highly polymorphic enzyme, were tested for reactivity against a panel of 295 placental extracts that had been typed electrophoretically. The products of the three common alleles as well as several rare alleles could be discriminated by the various antibodies. In some cases differences between allelic products were reflected by essentially 'all-or-none' reactions, but in other cases the differences were smaller and demonstrable only by quantitative analysis of the binding. Evidence for allelic differences not detectable electrophoretically was also obtained.",

author = "Slaughter, {C. A.} and Coseo, {M. C.} and Cancro, {M. P.} and H. Harris",

year = "1981",

doi = "10.1073/pnas.78.2.1124",

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AU - Slaughter, C. A.

AU - Coseo, M. C.

AU - Cancro, M. P.

AU - Harris, H.

PY - 1981

Y1 - 1981

N2 - Six monoclonal antibodies against human placental alkaline phosphatase [orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1], a highly polymorphic enzyme, were tested for reactivity against a panel of 295 placental extracts that had been typed electrophoretically. The products of the three common alleles as well as several rare alleles could be discriminated by the various antibodies. In some cases differences between allelic products were reflected by essentially 'all-or-none' reactions, but in other cases the differences were smaller and demonstrable only by quantitative analysis of the binding. Evidence for allelic differences not detectable electrophoretically was also obtained.

AB - Six monoclonal antibodies against human placental alkaline phosphatase [orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1], a highly polymorphic enzyme, were tested for reactivity against a panel of 295 placental extracts that had been typed electrophoretically. The products of the three common alleles as well as several rare alleles could be discriminated by the various antibodies. In some cases differences between allelic products were reflected by essentially 'all-or-none' reactions, but in other cases the differences were smaller and demonstrable only by quantitative analysis of the binding. Evidence for allelic differences not detectable electrophoretically was also obtained.

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Detection of enzyme polymorphism by using monoclonal antibodies

Abstract

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