By Kenneth R. Miller (Eds.)
As a self-discipline, cellphone biology has classically been outlined via the bounds which outline the boundaries of its pursuits. those limitations may possibly practice to place -cell biologists learn fabric in the mobile - or they might observe to dimension - cellphone biologists learn fabric above the extent of the macromolecule.
for a few years, the boundaries of strategy enforced those barriers as without doubt as any customized of the self-discipline. Our lack of ability to enquire buildings which can no longer be saw or molecules which may no longer be detected guaranteed that mobilephone biology wouldn't move the bounds which associated the mobile 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 example endlessly. cellphone biology at the present time crosses the boundary, hyperlinks the molecule with the organelle, affiliates the mobile reaction with the
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1985; Murray et al.. , 1986b). g.. a 150 kDa species found in heart) may be distinct N-CAM polypeptides. , 1988). In addition to the various forms of glycosylation, each N-CAM polypeptide undergoes other posttranslational modifiactions. In chicken, the Id and 32 BRUCE A. , 1984). , 1988). , 1985) presumably via a thioester linkage to a cysteine residue near the membranespanning region (Sefton and Buss, 1987). The sites phosphorylated in vilro are phosphorylated at very low levels in vivo; these sites are near those labelled at high levels in vivo or in organ culture; they are not phosphorylated unless the in vivo sites are occupied.
L-CAM has only three other cysteines. and these are widely distributed; one is in the precursor, one is at position 9, and the other is at position 449. The L-CAM sequence does not resemble the Ig superfamily in either the distribution of its cysteines or in its amino acid sequence. , 1987). In addition, there is no obvious correlation with the amino acid sequences of known calcium-binding sites of other calcium-bindingproteins. We assume that the calcium-binding sites of L-CAM are dependent on three-dimensional folding that brings otherwise disperse ligands into the proper configuration.