The JI
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     
 


The Journal of Immunology, 1976, 117: 91-96.
Copyright © 1976 by The American Association of Immunologists, Inc.

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Chang, C.-H.
Right arrow Articles by Angellis, D.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Chang, C.-H.
Right arrow Articles by Angellis, D.

Identification of a Butanol-Extractable Human Placenta-Specific Antigen with Alkaline Phosphatase Activity1

Chin-Hai Chang2 and Dennis Angellis

From the Tufts Cancer Research Center and The Department of Pathology, Tufts University School of Medicine, Boston, Massachusetts 02111

Abstract

n-Butanol extracts of whole-term placenta from different individuals were prepared, and used as immunogens to raise heterologous hyperimmune sera in rabbits. Upon immunoelectrophoresis the anti-placenta antisera could recognize at least six antigenic components in the placental extract even after they had been completely absorbed with pooled male serum proteins. However, the antisera so absorbed, designated (-PMS) antisera, could still react strongly with several normal adult tissue extracts including kidney. Systematic and quantitative absorptions of the (-PMS) antisera were thus further carried out with individual butanol extracts of normal adult liver, lung, intestine, stomach, kidney, bone, pancreas, spleen, heart, cerebrum, cerebellum, breast, and packed red cells, as well as a composite extract containing equal amounts of each of the 13 adult tissue extracts. Of the six antigenic components in the placental extracts reacting with the (-PMS) antisera the only one which retained its reactivity with the antisera throughout exhaustive absorptions was associated with alkaline phosphatase activity. This immunologic and enzymologic identity was confirmed with homogeneous placental alkaline phosphatase. Extracts from each of three placentae injected into three pairs of rabbits all produced an identical antibody reaction with the unique determinant(s) of placental alkaline phosphatase. The same identity of precipitin reaction was also found with extracts of 14 other placentae against each of these antisera. It thus firmly establishes that placental alkaline phosphatase is a characteristic placenta-specific fetal protein.

Footnotes

1 This investigation was supported by Grants in aid to Dr. W. H. Fishman from the National Cancer Institute, United States Public Health Service (CA-12924), Bethesda, Maryland, and from the Tobacco Research Council (935-M), New York.

2 To whom the correspondence should be addressed.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Website Copyright © 1976 by The American Association of Immunologists, Inc. All rights reserved.
All Contents Copyright © 1976 by The American Association of Immunologists, Inc. All rights reserved.