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J Kolodziej

Publications and source records attributed to J Kolodziej.

At least 19 recordsLinked to original sources

Human lung fructose-1,6-bisphosphatase is localized in pneumocytes II.

The localization of fructose-1,6-bisphosphatase (Fru-1,6-Pase EC 3.1.3.11) in human alveolar epithelium was determined immunohistochemically using a polyclonal antibody raised against the enzyme purified from human liver. The immunohistochemical analysis revealed that the Fru-1,6-Pase was localized in pneumocytes II and was absent in pneumocytes I. Hypothetically Fru-1,6-Pase participating in glucose-6-phosphate synthesis from noncarbohydrate precursors increases NADPH level which is used for surfactant synthesis and for glutathione redox cycle.

Animals↗

Surface topography dependent desorption of alkali halides

Electron-stimulated desorption of the (100)KBr surface has been investigated in vacuum with noncontact atomic force microscopy and mass spectroscopy. It has been found that both desorption components (K and Br) show oscillatory dependence on the electron dose with the oscillation amplitude decaying gradually. These results correspond with periodically varying, as a result of a layer-by-layer desorption, surface topography. It is proposed that the surface terrace edges act as traps for excited F centers diffusing in the crystal. The oscillating density of terrace edges varies surface recombination/reflection rates for the F centers and modulates the balance between surface and bulk deexcitation of the crystal.

Journal Article↗

cDNA sequence and kinetic properties of human lung fructose(1, 6)bisphosphatase.

A cDNA encoding fructose(1,6)bisphosphatase was isolated from total human lung RNA. The cDNA contained an open reading frame encoding 337 amino acids. The determined nucleotide sequence of the lung cDNA was significantly different from muscle cDNA and slightly differed from human liver cDNA in a single mutation (Gly-336 for Ala-336) and a T for C substitution in position 648. The human lung fructose(1, 6)bisphosphatase [Fru(1,6)Pase] was isolated and its kinetic parameters were compared with liver and muscle isoenzymes. Values of kcat for the lung Fru(1,6)Pase were lower than for the liver and muscle enzyme. Like the liver isoenzyme, lung Fru(1,6)Pase is significantly less inhibited by AMP than the muscle enzyme. The values of I0.5 were 9.5, 9.8, and 0.3 microM for the liver, lung, and muscle enzyme, respectively. The lung enzyme was slightly more sensitive to fructose(2,6)bisphosphate [Fru(2,6)P2] inhibition than the liver enzyme. Ki was 75 microM for the lung and 96 microM for the liver enzyme. The synergistic effect of AMP and Fru(2,6)P2 on the lung and liver Fru(1,6)Pase was also observed. In the presence of AMP the corresponding values of Ki for Fru(2,6)P2 were 16 microM for the lung and 10 microM for the liver enzyme.

Adenosine Monophosphate↗

Fine et al. Reply.

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Journal Article↗

Leiomyoma of the lung.

A case of asymptomatic pulmonary leiomyoma diagnosed by routine chest radiography and treated by lobectomy is reported. There is no particular clinical pattern that distinguishes this lesion, and diagnostic maneuvers to identify its nature are generally unrewarding except for biopsy. Resection is the recommended treatment.

Female↗