By J. David Robertson (auth.), Thomas E. Andreoli M.D., Joseph F. Hoffman Ph.D., Darrell D. Fanestil M.D., Stanley G. Schultz M.D. (eds.)
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N-acetylglucosaminidase to a lipid bilayer. Amino acid analyses of this protein show a composition of predominantly negatively charged residues with a low percentage of hydrophobicity, a property which it shares with egasyn. Several modified residues are present which may in part be associated with the lipid binding properties of ligatin. Again, in common with egasyn, ligatin is a glycoprotein and this is consistent with its location in the external leaflet of the plasma membrane. Another integral membrane protein studied extensively(214-220) is one embedded in the outer leaflet of the luminal membrane of the epithelial cells of the mammalian urinary bladder.
To test the validity of such interpretations, X-ray diffraction studies of retinal rod outer segment (ROS) membranes were begun. It was reasoned that if the transverse densities observed in ROS membranes were due either to phase transitions of the lipid or to protein molecules repeating regularly at a period of some 80-90 A, equatorial Bragg reflections from them should be easily detectable if meridional reflections from the lamellar repeat could be recorded. (153) Therefore, another explanation of the transverse densities was sought.
ISO) It is very interesting indeed that Paul and Goodenough(l49) have recently reported studies in which an antibody has been prepared to the MP26 protein from lens and used for immunocytological studies of preparations of lens membranes containing identifiable gap junctions in thin sections as well as wavy membranes, some of which are in close contact, and measure, according to them, 12 nm across. The antibodies were coupled to a fluorescent label for light microscopy and to ferritin for electron microscopy ofthin sections.
