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A Simplified Assay for Cryptococcal Phenoloxidase
Mycologia, 1986factor (Rhodes et al., 1982). The standard procedure for assaying phenoloxidase activity described by Polacheck et al. (1982) requires extensive sample preparation. Appropriately grown cells must be broken gently by vortexing with glass beads to minimize loss of activity and the membranes collected by ultracentrifugation.
Judith C Rhodes
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Phenoloxidases in ascidian hemocytes: characterization of the pro-phenoloxidase activating system
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2003The phenoloxidase (PO) activity of the hemocytes lysate supernatant from three ascidians species, assayed by means of 3-methyl-2-benzothiazolinone hydrazone hydrochloride, have been compared. PO-containing hemocytes were identified by a cytochemical reaction and the enzymatic activity measured by a spectrophotometric assay of lysate supernatant from ...
PARRINELLO, Nicolo' +4 more
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Temperature regulation of the cryptococcal phenoloxidase
Medical Mycology, 1991Melanin formation at 37 degrees C has been proposed as a virulence factor in Cryptococcus neoformans. However, whereas catecholamine uptake is maintained at this temperature, phenoloxidase, which catalyses the oxidation of catecholamine to melanin, is severely decreased in most wild type strains cultivated at 37 degrees C.
E S, Jacobson, H S, Emery
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Phenoloxidase of Mycobacterium leprae
Nature, 1967INVESTIGATIONS of the metabolism of Mycobacteriumleprae1 have revealed a few of the metabolic characteristics of this micro-organism. Concentrates of M. leprae prepared from lepromatous material actively oxidized 3,4-dihydroxyphenylalanine (DOPA) to pigmented products, in vitro2. Among several strains of mycobactena tested (including M. tuberculosis, M.
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Phenoloxidases of Aspergillus nidulans
Transactions of the British Mycological Society, 1974A maximum of five phenoloxidase bands of the tyrosinase type were detected on Polyacrylamide gels after disk electrophoresis of extracts of Aspergillus nidulans . One band could be distinguished from the others because it was thermolabile. At least one band was present in all samples analysed.
S.D. Martinelli, B.W. Bainbridge
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Properties of Phenoloxidase in Mycobacterium leprae
Nature, 1968Mycobacterium leprae separated from infected human tissues, oxidizes 3,4-dihydroxyphenylalanine (dopa) and a few other phenolic compounds1–3. This property is not shown by several other mycobacteria1,2,4. Phenoloxidase occurs in vertebrate melanocytes and is widely distributed in the plant kingdom5. (E.C.
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Multiple Forms of Phenoloxidase
Journal of Food Science, 1967SUMMARY— The phenoloxidase system in the tissues of mushrooms, potatoes, and apples was investigated using a polyacrylamide electrophoretic technique. The enzyme system was shown to exhibit the phenomenon of multiple forms.
S. M. CONSTANTINIDES, C. L. BEDFORD
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Processing of crayfish hemocyanin subunits into phenoloxidase
Biochemical and Biophysical Research Communications, 2004Hemocyanin and phenoloxidase are both copper-binding proteins involved in the immune system for a wide range of animal species. In crayfish, these proteins were purified and characterized from plasma and hemocytes, respectively. Recently, we have reported that the processing of one of the hemocyanin subunits occurs by a proteolytic cleavage under ...
So Young, Lee +2 more
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Molecular Forms of Apple Phenoloxidase
Biochemie und Physiologie der Pflanzen, 1979Summary Qualitative differences of dimeric (mol. wt. 60,000—70,000 D) and monomeric (mol. wt. 30,000 to 40,000 D) forms of phenoloxidase (EC 1.10.3.1) isolated from the fruits of two winter apple varieties were studied. It is shown that both forms differ distinctly by k m values and Hill coefficients.
M.N. Zaprometov +2 more
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