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


     
 


The Journal of Immunology, 1972, 109: 164-167.
Copyright © 1972 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 HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Day, N.
Right arrow Articles by Good, R. A.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Day, N.
Right arrow Articles by Good, R. A.

A Starfish Hemolymph Factor Which Activates Vertebrate Complement in the Presence of Cobra Venom Factor1

Noorbibi Day2, Hartmut Geiger3, Joanne Finstad4 and Robert A. Good5

From the Pathology Research Laboratories of the University of Minnesota Hospitals, Minneapolis, Minnesota 55455

Abstract

In recent studies we demonstrated the presence of a factor(s) in hemolymphs of invertebrates which interacts with purified cobra venom factor (CVF) and lyses erythrocytes in the presence of vertebrate serum or invertebrate hemolymph treated with EDTA (1). These CVF-reacting components were to some extent interchangeable between vertebrate sera and invertebrate hemolymph but the most marked hemolytic activity was observed when starfish (Asterius forbesi) hemolymph was reacted with purified CVF and added to frog serum in EDTA (1). In the present studies, we have isolated a factor(s) from starfish hemolymph and have shown that the purified product is capable of participating with CVF in activating the complement (C) system of the frog.

Materials and Methods. Vertebrate and invertebrate species. The frogs, Rana catesbeiana, were obtained from Schettles, Stillwater, Wis. The starfish (A. forbesi) were purchased from Marine Biological Laboratories, Woods Hole, Mass. The hemolymph was obtained from the starfish and then clarified according to methods described previously (1).

Footnotes

1 This work was supported by the National Foundation March of Dimes, American Heart Association and United States Public Health Service Grants AI-08677, AI-00798 and AI-10704.

2 Established Investigator of the American Heart Association.

3 Supported by Deutscher Akademischer Austauschdienst.

4 Research Associate in Pediatrics.

5 American Legion Memorial Research Professor, Regents' Professor of Pediatrics, Microbiology and Pathology.




This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
P. B. Armstrong, S. Swarnakar, S. Srimal, S. Misquith, E. A. Hahn, R. T. Aimes, and J. P. Quigley
A Cytolytic Function for a Sialic Acid-binding Lectin That Is a Member of the Pentraxin Family of Proteins
J. Biol. Chem., June 21, 1996; 271(25): 14717 - 14721.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Website Copyright © 1972 by The American Association of Immunologists, Inc. All rights reserved.
All Contents Copyright © 1972 by The American Association of Immunologists, Inc. All rights reserved.