[Comparative study of the amino acid and polysaccharide composition of the cell walls of mycocci and micrococci].
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Cyst walls isolated from Entamoeba invadens have a microfibrillar structure. The main sugars detected in acid hydrolysates from walls were hexosamines. X-ray diffraction analysis of the cyst walls demonstrated that the only crystalline polymer present was chitin.
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Effects of alkaline hydrogen peroxide (AHP) treatment on cellulose crystallinity and cell wall phenolic monomer and monosaccharide composition were measured using cotton and wheat straw (WS). Two WS treatments were used in this study, Type I WS, for which pH is not regulated during AHP treatment, and Type II WS, for which pH is regulated at 11.5 +/- .2 during AHP treatment. Wheat straw had a lower degree of cellulose crystallinity than cotton, but no differences occurred between treated and untreated substrates. Alkali-labile and nitrobenzene-extractable phenolic monomer concentrations were generally lower for Type I and Type II WS compared with untreated WS. Concentrations of glucose were higher and xylose and arabinose lower in Types I and II WS than in untreated WS. Disappearance of alkali-labile phenolic monomers and cell wall monosaccharides by wethers fed diets containing Type I (Exp. 1) or Type II (Exp. 2) AHP-treated WS were determined. Apparent digestibility of glucose and xylose before the duodenum, and of glucose, xylose and arabinose in the total tract, was greatest (P less than .05) when sheep were fed AHP-treated WS diets in both experiments. In Exp. 2, disappearance of alkali-labile phenolic monomers was greatest (P less than .05) before the duodenum and in the total tract when sheep were fed AHP-treated WS diets. Treatment of WS with AHP modified cell wall composition and increased cell wall monosaccharide digestion by sheep.
Analyses were made to determine the amino acid composition of the cell-wall proteins of Salmonella pullorum, S. senftenberg 775W, S. derby, and Escherichia coli. These proteins consist of the usual 18 amino acids found in most proteins with diaminopimelic acid in addition. Quantitative determination of these amino acids showed that their amounts were similar.