1. Capsaicin-Responsive NADH Oxidase Activities from Urine of Cancer Patients
- Author
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Dorothy M. Morré, S. Barogi, Ferda Yantiri, Kader Yagiz, Pin Ju Chueh, NaMi Cho, Sui Wang, D J Morré, and Dagmar Sedlak
- Subjects
Male ,medicine.drug_class ,Microgram ,Biophysics ,Urine ,Chemical Fractionation ,Monoclonal antibody ,Biochemistry ,chemistry.chemical_compound ,Multienzyme Complexes ,Neoplasms ,medicine ,Humans ,NADH, NADPH Oxidoreductases ,Molecular Biology ,Polyacrylamide gel electrophoresis ,Aged ,Chemistry ,Cancer ,medicine.disease ,Molecular biology ,Enzyme Activation ,Molecular Weight ,Ammonium Sulfate ,Capsaicin ,NADH oxidase ,Electrophoresis, Polyacrylamide Gel ,Female ,Digestion - Abstract
NADH oxidases of low specific activities from urine of cancer patients were found to be inhibited or stimulated by the vanilloid capsaicin (8-methyl-N-vanillyl-6-noneamide). Similar activities, inhibited or stimulated by capsaicin, were reported previously for sera of cancer patients but not for sera of normal volunteers or for patients with disorders other than cancer. Like those from sera, the activities from urine were resistant to heat and to digestion with proteinase K. Two different fractions with capsaicin-responsive NADH oxidase activities were obtained by FPLC. One fraction in which the 33-kDa band was the major component exhibited NADH oxidase activity stimulated by capsaicin. Another fraction in which 66-kDa and 45-kDa bands were major components exhibited NADH oxidase activities inhibited by capsaicin. A monoclonal antibody generated to a ca 34-kDa form of the NADH oxidase from sera reacted with a urine protein of a ca 33-kDa band in the capsaicin-stimulated fraction. The 33-kDa protein was of low abundance and was estimated to be present in amounts between 5 and 100 microgram/L, depending on the particular patient.
- Published
- 1998
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