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Fig. 1. Caenorhabditis elegans synthesize heparan sulfate proteoglycans. (A) Wild-type worms were incubated with radioactive sulfate and after solubilization in 4 M guanidine-HCl followed by dialysis against 8 M urea, were loaded onto a DEAE-Sephacel column of 1.0 ml bed volume, pre-equilibrated with the urea buffer. The column was washed and eluted using a linear gradient from 0.2 to 1.0 M NaCl. Aliquots of each fraction were counted (closed circles) and conductivity was determined (open circles). (B) Proteoglycans eluted from the DEAE indicated by the bar, were pooled, concentrated on a small DEAE column and fractionated on a Sepharose CL-6B column. The chromatographic profiles of control samples (closed circles), samples pre-incubated with proteinase K (open circles) and samples treated with alkaline borohydride to release the GAG chains (open triangles) are shown. (C) Proteoglycans eluted from the DEAE and concentrated as in B, were fractionated on a Sephadex G-50 column. The profiles shown correspond to untreated samples (closed diamonds) and samples previously incubated with either chondroitinase ABC (open triangles) or nitrous acid (open diamonds).
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