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Your search keyword '"J. P. Vandevoorde"' showing total 4 results
Start Over Author "J. P. Vandevoorde" Topic chemistry
4 results on '"J. P. Vandevoorde"'

1. Effect of Specific Anti-Sera on C14 Amino Acid Incorporation into Cellular Protein of Mouse Ascites Tumor Cells

Author

J. P. Vandevoorde, S. B. Nadler, Hans J. Hansen, and E. C. Hansen

Subjects
Cell, Protein metabolism, General Biochemistry, Genetics and Molecular Biology, Mice, chemistry.chemical_compound, Antigen, medicine, Animals, Neoplasm, Amino Acids, Antigens, Carcinoma, Ehrlich Tumor, chemistry.chemical_classification, Carbon Isotopes, biology, Immune Sera, Research, Carcinoma, Assay, Ascites, Proteins, Metabolism, medicine.disease, Molecular biology, Neoplasm Proteins, Amino acid, medicine.anatomical_structure, chemistry, Biochemistry, biology.protein, Antibody
Abstract

SummaryMouse ascites tumor cells exposed to specific anti-sera in the presence of complement failed to concentrate and incorporate labeled amino acid into gross cellular protein. Inhibition of amino acid uptake by specific anti-sera closely parallels cell rupture by anti-sera (in the presence of complement) and this appears to be a rapid and sensitive biochemical assay for antibody produced against mouse ascites tumor cells by the rat.

Published
1963
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2. Inhibition of J-128 (Osgood) cell culture by azaserine

Author

J. P. Vandevoorde and H. J. Hansen

Subjects
Guanine, Cell division, Chemistry, Adenine, Cell, Imidazoles, Nucleosides, DNA, Molecular biology, General Biochemistry, Genetics and Molecular Biology, Lesion, chemistry.chemical_compound, Tissue culture, medicine.anatomical_structure, Cell culture, Culture Techniques, medicine, Azaserine, Microscopy, Phase-Contrast, medicine.symptom, Hypoxanthine, medicine.drug
Abstract

SummaryAdenine, hypoxanthine or AICA will not reverse the inhibitory effect of aza-serine on the reproduction of J-128 cells in tissue cultures. Cells exposed to azaserine increase markedly in size with a parallel increase of nuclei size and DNA content. The drug appears to act quite similarly to certain mustards by stopping cell division between S and G2. A lesion appears in the central sphere of attraction in azaserine-treated cells, increases in size and apparently causes death of the cell.

Published
1966

3. METABOLISM OF LEUKEMIC CELLS IN CULTURE; AZASERINE INHIBITION OF J-128 (OSGOOD)

Author

J. P. Vandevoorde, S. B. Nadler, and Hans J. Hansen

Subjects
Purine, Guanine, Glycine, Biology, General Biochemistry, Genetics and Molecular Biology, Tissue Culture Techniques, chemistry.chemical_compound, Tissue culture, Nucleic Acids, medicine, Azaserine, Purine metabolism, Hypoxanthine, Pharmacology, Carbon Isotopes, Leukemia, Adenine, Imidazoles, Metabolism, medicine.disease, chemistry, Biochemistry, Purines, Hypoxanthines, Nucleic acid, medicine.drug
Abstract

SummaryOsgood's tissue culture J-128 may be cultured on a simple medium which does not contain preformed purine or AIC. When hypoxanthine or AIC are added to the culture medium the cells utilize th...

Published
1964

4. METABOLISM OF 9-ETHYL-6-MERCAPTOPURINE BY HUMANS

Author

W. G. Giles, S. B. Nadler, J. P. Vandevoorde, and Hans J. Hansen

Subjects
Drug, media_common.quotation_subject, 9-Ethyl 6-Mercaptopurine, Purine nucleoside phosphorylase, Pharmacology, Biology, General Biochemistry, Genetics and Molecular Biology, chemistry.chemical_compound, Glucosyltransferases, medicine, Humans, Xanthine oxidase, media_common, chemistry.chemical_classification, Carbon Isotopes, Chromatography, Leukemia, Mercaptopurine, Research, Nucleosides, Metabolism, Leukemia, Lymphoid, Rats, Enzyme, chemistry, Biochemistry, Liver, Spectrophotometry, Xanthines, Oxidoreductases, medicine.drug
Abstract

SummaryEvidence was presented that 9-E-6-MP is dealkylated by the human in amounts adequate to provide enough 6-MP to explain the effectiveness of this drug when it is administered to chronic granulocytic leukemia patients. 9-E-6-MP does not serve as substrate for xanthine oxidase, nor purine nucleoside phosphorylase. The possibility that the enzyme responsible for dealkylation is present in human bone marrow or neutro-phils is discussed.

Published
1964

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