By Kenneth R. Miller (Eds.)
As a self-discipline, phone biology has classically been outlined via the limits which outline the boundaries of its pursuits. those obstacles might observe to place -cell biologists research fabric in the cellphone - or they could follow to measurement - mobile biologists research fabric above the extent of the macromolecule.
for a few years, the boundaries of process enforced those obstacles as absolutely as any customized of the self-discipline. Our lack of ability to enquire buildings that could now not be saw or molecules that could now not be detected guaranteed that cellphone biology wouldn't go the limits which associated the cellphone to different degrees of association. because the 20th century nears its shut, besides the fact that, the advance of a tremendous diversity of instruments and strategies, a few actual, a few chemical, a few organic, has replaced this example eternally. mobilephone biology at the present time crosses the boundary, hyperlinks the molecule with the organelle, affiliates the mobile reaction with the
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Schematic drawing of N-CAM (A) in terms of the amino acid sequences of the three polypeptides (B). Loops I-V (A) indicate disulfidebonded segments (C-C in B) that resemble immunoglobulin domains. The stippled vertical bar in A denotes the plasma membrane. The shaded portion of A indicates the membrane-spanning regions (thick underline in B) of the sd and Id chains and the carboxyl terminus unique to the ssd chain is indicated separately in both A and B. The slashed portion of A represents the cytoplasmic domains of the Id and sd polypeptides and the sequence unique to the Id chain indicated in A is outlined by the large box in B.
34: 470a. Shen. B.. Josephs. R.. and Steck. T. L. (1986) J. Cell Biol. 102 997-1006. Siegel. D.. and Bianton, D. (1985) J. Cell Biol. 100: 775-785. Smith. B. D.. LaCelle. P. L.. Siefring, G. E.. Lowe-Krentz. L.. and Lorand. L. (1981) J. Membrane Biol. 61: 75-80. Steck. T. L. (1974) J. Cell Biol. 6 2 1-19. Tao. M.. Conway. R.. and Cheta. S. (1980) J. Biol. Chem. 255: 2563. Thomas. E. L.. King, L. , and Morrison, M. (1979) Arch. Biochem. Biophys. 1%: 454-464. Tyler. J. M.. Hargreaves. W.. and Branton, D.
Components of M, 100,000 are also detected in L-CAM preparations and immunoprecipitates; some of these may be L-CAM fragments, but others appear to be associated molecules of undetermined significance. , 1983) (Figure 4B). Ftl has the same amino terminus as the intact molecule as found on the cell surface. , 1984). The intact protein, but not Ftl, can be phosphorylated on threonine and serine residues. All of these data indicate that L-CAM is an integral membrane protein with the amino terminus on the exterior side of the membrane and the carboxyl terminus on the cytoplasmic side.
A Research Annual by Kenneth R. Miller (Eds.)