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  • Book
    Narsing A. Rao, Julie Schallhorn, Damien C. Rodger, editors.
    Summary: This comprehensive text provides readers with an in-depth examination of posterior uveitis, and expert instruction on diagnosis, imaging techniques and treatments that are being reshaped by advancements in the field. Posterior Uveitis: Advances in Imaging and Treatment focuses on the ocular imaging modalities used in the diagnosis of various uveitis and intraocular inflammation entities resulting from infectious and non-infectious etiologies. Each topic is succinctly presented by experts in the field of intraocular inflammation and ocular imaging and starts with salient clinical features, differential diagnosis and specific treatment, and concludes with in-depth and relevant clinical imaging findings. The book opens by touring a multitude of infectious and non-infectious uveitidies and explores how advances are aiding our diagnosis and treatment. The second half will delve into established and emerging therapeutics, including advances in drug delivery. Evolving treatments for recalcitrant uveitis are discussed, including the newer biological agents, and each chapter includes ample illustrations and several tables for readers to comprehend with ease the inflammatory disorders and to interpret the imaging changes in various uveitis entities.
    Digital Access Springer 2019
  • Article
    Alderete JF, Robertson DC.
    Infect Immun. 1978 Mar;19(3):1021-30.
    Heat-stable enterotoxin (ST) produced by porcine strains of enterotoxigenic (ENT+) Escherichia coli has been purified to apparent homogeneity by sequential ultrafiltration, acetone fractionation, preparative gel electrophoresis, diethylaminoethyl Bio-Gel A ion-exchange chromatography, and Bio-Gel P-10 gel filtration. The enterotoxin, purified more than 1,500-fold, exhibited a molecular weight of 4,400, as determined by both sodium dodecyl sulfate-gel electrophoresis and gel filtration. A molecular weight of 5,100, representing 47 residues, was calculated from amino acid analysis data. The amino acid content was distinctive, with an unusually high proportion of cystines and few hydrophobic amino acids. A single amino-terminal residue, glycine, was observed. Purified ST was stable to heating (100 degrees C, 30 min) and did not lose biological activity after treatment with Pronase, trypsin, proteinase K, deoxyribonuclease, ribonuclease, and phospholipase C. Periodic acid oxidation and several organic solvents (acetone, phenol, chloroform, and methanol) had no effect on the biological activity of ST. Further, purified ST was stable to acid treatment at pH 1.0 but lost biological activity at pH values greater than 9.0. Neither lipopolysaccharide nor lipid contamination was evident in purified preparations. A characteristic absorption spectrum was observed during the course of the purification, which shifted from a maximum at 260 nm in crude preparations to 270 nm for the purified toxin. Antiserum obtained from rabbits immunized with ST or ST coupled to bovine serum albumin neutralized the action of the enterotoxin in suckling mice; however, passive hemagglutination and hemolysis titer assays suggested that ST is a poor antigen.
    Digital Access Access Options