By Kenneth R. Miller (Eds.)
As a self-discipline, cellphone biology has classically been outlined through the limits which outline the boundaries of its pursuits. those obstacles might follow to place -cell biologists learn fabric in the mobile - or they could practice to measurement - phone biologists learn fabric above the extent of the macromolecule.
for a few years, the boundaries of process enforced those barriers as definitely as any customized of the self-discipline. Our lack of ability to enquire constructions that could now not be saw or molecules which can no longer be detected guaranteed that cellphone biology wouldn't move the bounds which associated the mobilephone to different degrees of association. because the 20th century nears its shut, notwithstanding, the advance of a big variety of instruments and strategies, a few actual, a few chemical, a few organic, has replaced this case ceaselessly. mobile biology at the present time crosses the boundary, hyperlinks the molecule with the organelle, affiliates the mobile reaction with the
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J.. Ungewickell. E.. Calvert. , and Gratzer. W. B. (1979) FEBS Lett. 104: 396-400. Plut. D. A.. Hosey. M. M.. and Tao, M. (1978) Eur. J. Biochem. 8 2 333-337. Quist, E. , and Roufogalis, 8. D. (1975) Arch. Biochem. Biophys. 168 240-251. Raval. P. J.. an1 Allan, D. (1985) Biochem. J. 232 4 3 4 7 . Rybicki. , and Schwartz. R. S. (1985) J. Supramol. Struct. 98: 18. Sarkadi. , Szasz. I.. and Gardos. G. (1976) J. Membr. Biol. 26: 357-370. Schwartz. R. , Rybicki. A. , Mohandas. N.. Wolf. J. , and Lubin, B.
1987). , 1984). Hoffman and B. A. Cunningham, unpublished observations). The polysialic acid could be on any or all of the three potential sites. Because two (404 and 459) are close to the cysteines and the other (430) is in the center of the presumed disulfide loop, all three would be on the surface of the molecule if this region folds like an immunoglobulindomain (Edelman, 1970 Amzel and Poljak, 1979). From residue 500 to the membrane (690) there are no cysteines. The most prominent homology is with the cell-binding domain of fibronectin.
Biol. Chem. 260: 46-49. Woodget. J. R.. and Hunter, J. (1987) J. Biol. Chem. 262 4836-4843. THE STRUCTURE AND FUNCTION OF CELL ADHESION MOLECULES Bruce A. Cunningham OUTLINE I. 11. 111. IV. V. INTRODUCTION N-CAM A. Amino Acid Sequence B. mRNAs and the N-CAM Gene L-CAM AND RELATED MOLECULES Ng-CAM AND OTHER SECONDARY CAMS GENERAL CONSIDERATIONS REFERENCES Advances in Cell Biology, Volume 2, pages 25-54. Copyright 8 1988 by JAI Ress Inc. All rigbb of reproductioa in my fonn reserved. ISBN: 0-89232-886-X 25 25 28 33 38 40 46 48 49 BRUCE A.