Biomedical subjects
Publications and source records attributed to W E Inniss.
A simple modification of Gray's flagellar staining procedure is described. It can be used on air-dried smears or directly on wet mounts of motile bacteria. The stained bacterial flagella can be observed with phase-contrast or bright-field optics. No rigorous cleaning of slides, counterstains, or any washing procedures are required with the staining method, making it very suitable for routine examinations.
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The fine structure of lipopolysaccharide (LPS), isolated from an avian strain of Escherichia coli O18, was examined by electron microscopy. In positively stained preparations, ribbonlike structures with frequent branching were observed as previously reported (4). Two densely stained parallel lines were occasionally seen associated with a ribbon. When negative staining was employed, the LPS appeared as a branching ribbon with one central and two lateral zones divided by two relatively dense parallel lines running the complete length of the ribbon. The lateral zones were probably due to the O-antigenic side chains of the LPS. This interpretation was supported by the fact that the electron microscopic structure of the LPS from two rough strains, E. coli K-12 Gal 23 and Salmonella tuphimurium TV119 RII, both lacking the O-specific side chains, did not possess the outer lateral zones.
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Polymxyin treatment of isolated lipopolysaccharide from Escherichia coli resulted in the breakdown of its structure.
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Inniss, William E. (Michigan State University, East Lansing) and Charles L. SanClemente. Biochemical studies on staphylocoagulase and an allied phosphatase activity. J. Bacteriol. 83:941-947. 1962.-The present investigation was undertaken to determine whether the reported correlation between the coagulase and phosphatase activity of the staphylococci was functional. Staphylococcus aureus, phage-propagating strain 70, grown in brain heart infusion was the source of the purified coagulase. The concomitant phosphatase activity, measured spectrophotometrically at 400 mmu using p-nitrophenylphosphate as substrate, showed a parallel decrease during thermal inactivation at 37 and 56 C. Anion-exchange chromatography and electrophoresis using starch, starch gel, and paper as stabilizing media failed to separate the two activities. Since iodoacetate, ethylenediamine-tetraacetate, fluoride, azide, and p-chloromercuribenzoate always exerted different degrees of inactivation, apparently the same mechanism was not involved. This supposition was supported by subsequent saturation of the phosphatase with excess substrate (100-fold K(s) value) and the demonstration that under this condition coagulase was not inhibited. During this purification process, comparable increases in specific activity occurred for both coagulase and phosphatase, indicating the presence of a common protein carrier.