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D Stancek

Publications and source records attributed to D Stancek.

52 records · Page 3Linked to original sources
PubMed1971

Preparative electrophoresis of isotopically labeled L-cell interferons.

The preparative method of polyacrylamide gel electrophoresis was adapted for purification and characterization of isotopically labeled L-cell interferons. Re-covery of interferon activity was quantitative, and purification and resolution were comparable to those obtained by analytical polyacrylamide gel electrophoresis. Ultimate specific activities attainable ranged from 2 x 10(6) to 3 x 10(6) international units per mg of protein.

Biological Assay↗
PubMed1971

Structural proteins of rabies virus.

Purified rabies virions, unlabeled or labeled with radioactive amino acids or d-glucosamine, were dissociated into their polypeptides by treatment with sodium dodecyl sulfate in a reducing environment and fractionated by electroiphoresis in sodium dodecyl sulfate-containing polyacrylamide gel. The molecular weights of individual polypeptides were estimated by comparison of their rate of migration with that of protein markers of known molecular weight. Purified viral nucleocapsid and a mixture of envelope components, isolated from virions disrupted by sodium deoxycholate, were analyzed by the same procedure. The number of molecules per virion of each polypeptide was estimated from the proportions of the separated components, the known molecular weight of the viral ribonucleic acid, and the chemical composition of the nucleocapsid. The protein moiety of the nucleocapsid particle was estimated to consist of 1,713 molecules of a major polypeptide (molecular weight, 62,000 daltons) and 76 molecules of a minor polypeptide (molecular weight, 55,000 daltons). In addition to 1,783 molecules of a glycoprotein component (molecular weight, 80,000 daltons), the viral envelope contains 789 and 1,661 molecules, respectively, of two other polypeptides (molecular weight, 40,000 and 25,000 daltons).

Amino Acids↗
PubMed1970

Purification, characterization, and attempts at isotopic labeling of mouse interferon.

Under optimal conditions which minimized the accumulation of extraneous proteins, interferon preparations were obtained in L cells containing from 2 x 10(4) to 5 x 10(4) units/mg of protein. The radiolabeled proteins were liberated simultaneously with interferon from cultures exposed to tritiated amino acids after viral stimulation and from corresponding controls, and were subsequently purified with the following results. Chromatography of interferon on carboxymethyl-Sephadex C-25 eliminated selectively unlabeled or poorly labeled proteins, resulting in a greater than sixfold increase in counts per minute per milligram of protein. Similarly purified control material harbored at least 12 times less tritium per milligram of protein than interferon, and the label was more diversely distributed among proteins of different molecular weights. On electrophoresis of interferon in polyacrylamide gels, labeled proteins were reduced further by a factor of at least 10 without loss in titer. Final purification was estimated at greater than 280-fold, representing a calculated specific activity of at least 1.4 x 10(7) units of interferon per milligram of protein.

Acrylates↗
PubMedDate not supplied

[Etiological and immunopathological markers in hepatitis B patients in the early convalescence stage during the development of chronic liver involvement].

Etio- and immunopathological markers in hepatitis B are analysed. Combinations of specific HB markers in a highly aggressive process are characterized in comparison with the lack of this aggressiveness. Among immunopathological markers, most informative were the levels of C3 component of complement and of immunocomplexes from the point of view of acute hepatitis B prognosis. The frequency and features of mixed hepatitis infection: HA and HB, HB and delta-infection are discussed.

Adolescent↗