Bound sugars in hepatic glycoproteins from male rats during early protein depletion
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One purpose of these experiments was to determine whether qualitative changes take place in the attached components of hepatic (post-mitochondrial) glycoproteins isolated from rats fed a low protein diet (5% casein) for one week. In the "acid-insoluble" fraction (I) no significant changes in bound fucose, galactose, mannose, total hexosamines and sialic acid were seen after early depletion. It should be noted however that the largest change was a decrease in the bound mannose. An isotope study showed a statistical decrease in the level of labeled (1–14C) mannose incorporation in vitro (cpm per mgm protein) but no difference was found if the data is expressed as cpm per mgm bound mannose of (I). In the more sugar-rich "acid-soluble" fraction (S) significant increases in both bound mannose and glucose were seen with no change in the fucose levels; none of the other bound carbohydrates seen in (I) were found in (S). In a similar isotope study using mannose no differences in the rat or level of uptake (cpm per mgm of mannose or protein) in (S) was seen. The data favors an interpretation that, following early protein depletion, there is an apparent overall increase in sugar-rich glycoproteins in (S). The question still remains to whether there is increase in the population of specific mannose and glucose rich glycoproteins or whether more carbohydrate branching occurs in (S). In any case, an adaptive phenomenon is indicated for maintaining the intracellular environment during periods of inadequate amino acid supply.
PLEASE NOTE: This work is protected by copyright. Downloading is restricted to the BU community: please click Download and log in with a valid BU account to access. If you are the author of this work and would like to make it publicly available, please contact firstname.lastname@example.org.Thesis (M.S.)--Boston University, Henry M. Goldman School of Graduate Dentistry, 1979, (Nutritional Sciences)Bibliography: leaves 55-68.
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