Binding of alpha-fetoprotein by immobilized monoclonal antibodies during episodes of zero-gravity obtained by parabolic flight.
Alpha-fetoprotein (AFP), a single chain polypeptide which is synthesized by the liver and yolk sac of the human fetus, provided a model ligand for assessing the effects of microgravity on ligand binding to surface-immobilized model receptor molecules. Monoclonal antibodies, used as receptors for AFP, were immobilized by covalent attachment to latex microparticles. Zero gravity environment was obtained by parabolic flight aboard NASA 930, a modified KC-135 aircraft. During the onset of an episode of zero gravity, ligand and receptor were mixed. Timed incubation (20 s) was terminated by centrifugation, the supernatant removed, and microparticles were assessed for bound AFP by immunochemical methods. The extent of binding was not influenced by microgravity, when compared with 1-G controls, which suggests that aberrant cellular activities observed in microgravity are not the simple expression of altered macromolecular interactions.
BioServe Space Technologies, Kansas State University, Manhattan 66506.
B S
BS
Spooner
J A
JA
Guikema
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G
Barnes
D000911:Antibodies, Monoclonal; D002214:Capsules; D006112:Gravitation; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D011485:Protein Binding; D011956:Receptors, Cell Surface; D013026:Space Flight; D013499:Surface Properties; D000509:alpha-Fetoproteins / Q000378:metabolism*
D000911:Antibodies, Monoclonal; D002214:Capsules; D008024:Ligands; D011956:Receptors, Cell Surface; D000509:alpha-Fetoproteins