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Isolation and characterization of sea star factor
Scandinavian Journal of Immunology
|January 1, 1976
Summary
Sea star factor (SSF) inhibits immune responses and cell growth. This potent inhibitor, a purified protein, binds to a unique site distinct from concanavalin A, offering insights into immune regulation.
Area of Science:
- Immunology
- Marine Biology
- Biochemistry
Background:
- Sea star factor (SSF) from Asterias forbesi celomocytes is known to inhibit immune responses.
- It also suppresses mitogenesis induced by concanavalin A, a common immune stimulant.
Purpose of the Study:
- To isolate and purify the protein responsible for SSF's biological activities.
- To characterize the purified protein and investigate its binding properties.
Main Methods:
- Isolation and purification of a basic protein from sea star celomocytes.
- Determination of molecular weight and subunit composition via reduction.
- Binding assays using spleen cells, concanavalin A, and labeled/unlabeled SSF.
Main Results:
- A basic protein with a molecular weight of approximately 38,000 daltons was isolated and purified.
- This protein was identified as the active component responsible for inhibiting immune responses and mitogenesis.
- Binding studies indicated that SSF binds to a site distinct from the concanavalin A binding site on spleen cells.
Conclusions:
- The purified protein, sea star factor, is a potent inhibitor of T-dependent immune responses and concanavalin A-induced mitogenesis.
- The data suggest a unique binding mechanism for SSF, separate from that of concanavalin A, implying a novel pathway for immune modulation.