Phytohemagglutinin and transmembrane proteins in agglutinated sheep erythrocyte ghost membranes.
Oriented and periodically stacked sheep erythrocyte ghost membrane specimens were prepared by agglutination of the ghosts with phytohemagglutinin M and sedimentation, and were studied by X-ray diffraction. The spatial orientation of the planes of the membranes in the diffracting stack was determined from the lamellar reflections of the periodic stacking. Equatorial diffraction at (10.5 A)-1 and a (1.5 A)-1 reflection were recorded which correlate with side-to-side packed transmenbrane alpha-helices in the agglutinated membrane. A broad (4.6 A)-1 ring with strong equatorial accentuation and broad maxima at about (2.2 A)-1 and (1.2 A)-1 were observed which are attributed to the hydrocarbon chain arrangement in lipid phases of the agglutinated ghost membrane.
D000818:Animals; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D006384:Hemagglutination / Q000187:drug effects*; D066298:In Vitro Techniques; D037102:Lectins / Q000494:pharmacology*; D008563:Membrane Lipids / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism*; D011487:Protein Conformation; D012756:Sheep; D014961:X-Ray Diffraction
D037102:Lectins; D008563:Membrane Lipids; D008565:Membrane Proteins