Raymond Schmitt

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Partial sequence analysis of tryptic peptides has identified the E1B-495R (E1b-57K) (early transcription region 1B of 495 amino acid residues, with an approximate molecular weight of 57,000) protein of adenovirus 2 as encoded by the 495 amino acid open reading frame located in the adenovirus 2 DNA sequence between nucleotides 2016 and 3500. Additional(More)
The effects of plasma Cu(II) ligands on the kinetics of Cu(II) transport by rat liver parenchymal cells were determined to examine how Cu(II) is mobilized from plasma and transported into liver cells. Albumin markedly inhibited Cu(II) uptake at Cu(II)-to-albumin molar ratios of 3:1 or less. Kinetic analyses showed that albumin inhibits Cu(II) uptake by(More)
The kinetics of copper efflux from rat hepatocytes were determined to further characterize the hepatic Cu(II) transport system. Efflux was biphasic. Net efflux was rapid for 1-5 min, and 35-45% of preloaded copper was lost by 40 min. Efflux was negligible after 40 min. The retained percentage was independent of the preloading concentration, but the total(More)
The effects of plasma components on the kinetics of copper transport by rat hepatocytes were examined in an attempt to determine how copper is mobilized from plasma for uptake by the liver. Specific protein-facilitated transport was indicated by saturation kinetics, competition by related substrates, and similar kinetic parameters for uptake and efflux. For(More)
Uptake and efflux of 64Cu were examined to determine whether hepatic parenchymal cells exhibit the kinetic criteria of a specific transport system for copper and related trace metals. Saturation kinetics were clearly indicated by both v versus [Cu] and 1/v versus 1/[Cu] plots (Km = 11 +/- 0.6 microM and Vmax = 2.7 nmol Cu X min-1 X mg prot-1). Identical(More)
A 1966 article by the senior, based on 1948--1952 census tract data for the Honolulu SMSA, reported a colse correlation between resident population densities and various health and social disorganization rates, even when persons per room, educational level, and income were controlled. The present study, based largely on 1974 tract data for the same SMSA,(More)
The localization in infected and transformed cells of the two major adenovirus type 2 E1a proteins, of 289 and 243 amino acid residues, was studied with antisera raised against synthetic peptides or a TrpE-E1a fusion protein. Both E1a proteins were detected only in the nucleus of infected cells as determined by immunofluorescence analysis of cells infected(More)