Uterine estrogen induced protein: physical and immunological comparison with ovalbumin

B. S. Katzenellenbogen, L. B. Williams

Research output: Contribution to journalArticle

Abstract

The physical and immunological properties of the estrogen induced protein from rat uterus are compared with those of ovalbumin from chick oviduct. Both proteins are induced by estrogen and are under estrogenic regulation. Electrophoretic mobility on sodium dodecyl sulfate polyacrylamide gels and elution behavior on Sephadex G 100 column chromatography indicate that the uterine protein has a molecular weight of about 42,000, similar to that of ovalbumin, and likewise is composed of only one subunit. On isoelectric focusing in polyacrylamide gels, both proteins focus at a pH of 4.6. The uterine protein, in addition, shows a component with an isoelectric point of 5.1. Despite considerable similarity in the physical properties of the uterine protein and ovalbumin, there is no significant crossreactivity of antiovalbumin gamma globulin with the uterine protein, implying that these 2 estrogen regulated proteins are immunologically distinct.

Original languageEnglish (US)
Pages (from-to)1281-1285
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume71
Issue number4
DOIs
StatePublished - Jan 1 1974

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Ovalbumin
Estrogens
Proteins
Oviducts
gamma-Globulins
Isoelectric Point
Isoelectric Focusing
Sodium Dodecyl Sulfate
Uterus
Chromatography
Molecular Weight

ASJC Scopus subject areas

  • General

Cite this

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abstract = "The physical and immunological properties of the estrogen induced protein from rat uterus are compared with those of ovalbumin from chick oviduct. Both proteins are induced by estrogen and are under estrogenic regulation. Electrophoretic mobility on sodium dodecyl sulfate polyacrylamide gels and elution behavior on Sephadex G 100 column chromatography indicate that the uterine protein has a molecular weight of about 42,000, similar to that of ovalbumin, and likewise is composed of only one subunit. On isoelectric focusing in polyacrylamide gels, both proteins focus at a pH of 4.6. The uterine protein, in addition, shows a component with an isoelectric point of 5.1. Despite considerable similarity in the physical properties of the uterine protein and ovalbumin, there is no significant crossreactivity of antiovalbumin gamma globulin with the uterine protein, implying that these 2 estrogen regulated proteins are immunologically distinct.",
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N2 - The physical and immunological properties of the estrogen induced protein from rat uterus are compared with those of ovalbumin from chick oviduct. Both proteins are induced by estrogen and are under estrogenic regulation. Electrophoretic mobility on sodium dodecyl sulfate polyacrylamide gels and elution behavior on Sephadex G 100 column chromatography indicate that the uterine protein has a molecular weight of about 42,000, similar to that of ovalbumin, and likewise is composed of only one subunit. On isoelectric focusing in polyacrylamide gels, both proteins focus at a pH of 4.6. The uterine protein, in addition, shows a component with an isoelectric point of 5.1. Despite considerable similarity in the physical properties of the uterine protein and ovalbumin, there is no significant crossreactivity of antiovalbumin gamma globulin with the uterine protein, implying that these 2 estrogen regulated proteins are immunologically distinct.

AB - The physical and immunological properties of the estrogen induced protein from rat uterus are compared with those of ovalbumin from chick oviduct. Both proteins are induced by estrogen and are under estrogenic regulation. Electrophoretic mobility on sodium dodecyl sulfate polyacrylamide gels and elution behavior on Sephadex G 100 column chromatography indicate that the uterine protein has a molecular weight of about 42,000, similar to that of ovalbumin, and likewise is composed of only one subunit. On isoelectric focusing in polyacrylamide gels, both proteins focus at a pH of 4.6. The uterine protein, in addition, shows a component with an isoelectric point of 5.1. Despite considerable similarity in the physical properties of the uterine protein and ovalbumin, there is no significant crossreactivity of antiovalbumin gamma globulin with the uterine protein, implying that these 2 estrogen regulated proteins are immunologically distinct.

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