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Biomedical subjects

S Seltzer

Publications and source records attributed to S Seltzer.

14 recordsLinked to original sources
PubMed1977

Correlation of scanning electron microscope and light microscope findings in uninflamed and pathologically involved human pulps.

The use of the scanning electron microscope has been investigated as a modality for pulpal diagnosis. Findings in ten normal, inflamed, and necrotic human pulps were correlated with light microscope findings. Inflammatory cell identification by SEM was found to be difficult. The inflammatory cells, especially lymphocytes, appeared in varying forms in SEM. Polymorphonuclear leukocytes and macrophages had similar surface structure. Degenerative changes of cells and fibers and dystrophic mineralizations were graphically depicted by SEM.

Abscess↗
PubMed1977

Endodontic classification.

Clinical and histopathologic findings are mixed in current endodontic classifications. A new system, based on symptomatology, may be more useful in clincial practice. The classifications are vital asymptomatic, hypersensitive dentin, inflamed-reversible, inflamed/dengenerating without area-irreversible, inflamed/degenerating with area-irreversible, necrotic without area, and necrotic with area.

Acute Disease↗
PubMed1976

Maleylacetone cis-trans-isomerase: affinity chromatography on glutathione-bound sepharose. Two-substrate-binding sequence from inhibition patterns.

Maleylacetone cis-trans-isomerase isolated from Vibrio 01 binds glutathione strongly; Km = 1.4 X 10(-4) M. Oxidized glutathione and S-methylglutathione are competitive inhibitors, KI = 9.4 X 10(-4) and 1.2 X 10(-3) M, respectively. Based on these interactions, three different glutathione-bound agarose affinity adsorbents were synthesized and tested. Affinity chromatography of the isomerase with one of these affords 70- to 100-fold purifications. In separate syntheses, portions of the affinity arm were prepared and examined as to their inhibitory properties in the enzyme-catalyzed reaction. The fragment, containing glutathione bound through its sulfur to the carbon chain, is a powerful competitive inhibitor for glutathione (KI = 6 X 10(-5) M). The results described suggest that the isomerase binds glutathione through the backbone of the tripeptide and that the thiol group is required for activity. The initial velocity patterns of the enzyme-catalyzed reaction resulting from simultaneous variation of glutathione and maleylacetone concentrations were examined in the absence and presence of inhibitors resembling glutathione. The observed kinetic patterns suggest an ordered sequence of binding maleylacetone first followed by glutathione.

Binding Sites↗