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Proteoglycan subunit

Figure 48-6. Dark field electron micrograph of a proteoglycan aggregate in which the proteoglycan subunits and filamentous backbone are particularly well extended. (Reproduced, with permission, from Rosenberg L, Heilman W, Kleinschmidt AK Electron microscopic studies of proteoglycan aggregates from bovine articular cartilage. J Biol Chem 1975 250 1877.)... Figure 48-6. Dark field electron micrograph of a proteoglycan aggregate in which the proteoglycan subunits and filamentous backbone are particularly well extended. (Reproduced, with permission, from Rosenberg L, Heilman W, Kleinschmidt AK Electron microscopic studies of proteoglycan aggregates from bovine articular cartilage. J Biol Chem 1975 250 1877.)...
Figure 4-16 (A) Dark field electron micrograph of a proteoglycan aggregate from bovine articular cartilage (from bearing surfaces of joints). Courtesy of Joseph A. Buckwalter. The filamentous backbone consists of hyaluronic acid, as in (B). The proteoglycan subunits extend from the backbone. From Rosenberg.149... Figure 4-16 (A) Dark field electron micrograph of a proteoglycan aggregate from bovine articular cartilage (from bearing surfaces of joints). Courtesy of Joseph A. Buckwalter. The filamentous backbone consists of hyaluronic acid, as in (B). The proteoglycan subunits extend from the backbone. From Rosenberg.149...
Roughley PJ, White RJ. Age-related changes in the structure of the proteoglycan subunits from human articular cartilage. J Biol Chem 1980 255 217-224. [Pg.148]

Melching LI, Roughley PJ. Studies on the interaction of newly secreted proteoglycan subunits with hyaluronate in human articular cartilage. Biochim Biophys Acta Gen Subj 1990 1035 20-28. [Pg.150]

Structural Characterization of Proteoglycan Subunit from Nasal Septum by Laser Light Scattering... [Pg.201]

Solution studies of proteoglycan subunit are described. In dilute aqueous NaCl, self-association behavior of subunit is observed which occurs at the globular protein hook region. Thus the association is banished by denaturation with guanidine hydro-... [Pg.211]

The PI anchor maintains adhesion of acetylcholinesterase (of the red blood cell) and of some proteoglycans (su I fated proteinsof the extracellular matrix) to the cell membrane Palmitic acid is bound via thiol-ester bonds toCys 322 and Cys 323 of rhodopsln (see the section on vitamin A), a 327-amino-add protein. The polypeptide chain of rhodopsin loops in and out of the membrane several times, leaving the possible function of the lipid as an anchor in question. Myristic add is bound to the catalytic subunit of the cAMP-dependent protein kinase, though this protein is cytosolic and soluble. [Pg.325]


See other pages where Proteoglycan subunit is mentioned: [Pg.293]    [Pg.80]    [Pg.115]    [Pg.181]    [Pg.29]    [Pg.193]    [Pg.303]    [Pg.181]    [Pg.169]    [Pg.201]    [Pg.203]    [Pg.205]    [Pg.291]    [Pg.294]    [Pg.298]    [Pg.292]    [Pg.301]    [Pg.293]    [Pg.80]    [Pg.115]    [Pg.181]    [Pg.29]    [Pg.193]    [Pg.303]    [Pg.181]    [Pg.169]    [Pg.201]    [Pg.203]    [Pg.205]    [Pg.291]    [Pg.294]    [Pg.298]    [Pg.292]    [Pg.301]    [Pg.79]    [Pg.24]    [Pg.115]    [Pg.437]    [Pg.1883]    [Pg.359]    [Pg.194]    [Pg.136]    [Pg.324]    [Pg.40]    [Pg.205]    [Pg.132]    [Pg.307]    [Pg.160]    [Pg.220]    [Pg.555]    [Pg.144]    [Pg.226]    [Pg.575]    [Pg.134]    [Pg.970]    [Pg.911]    [Pg.949]    [Pg.14]   
See also in sourсe #XX -- [ Pg.201 ]




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Proteoglycan Proteoglycans

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