Results 171 to 180 of about 12,945 (227)

Properties of Phenoloxidase in Mycobacterium leprae

Nature, 1968
Mycobacterium 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.
exaly   +3 more sources

Changes in lipophorins are related to the activation of phenoloxidase in the haemolymph of Locusta migratoria in response to injection of immunogens [PDF]

Insect Biochemistry and Molecular Biology, 2003
In Locusta migratoria, activation of phenoloxidase in the haemolymph in response to injection of laminarin is age-dependent: being absent in fifth instar nymphs and newly emerged adults, and only becoming evident four days after the final moult.
Goldsworthy, Graham J., Mullen, Lisa M.
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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, 2003
The 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', ARIZZA, Vincenzo, Chinnici, C, PARRINELLO, Daniela, CAMMARATA, Matteo   +4 more
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Temperature regulation of the cryptococcal phenoloxidase

Medical Mycology, 1991
Melanin 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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Phenoloxidases of Aspergillus nidulans

Transactions of the British Mycological Society, 1974
A 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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Multiple Forms of Phenoloxidase

Journal of Food Science, 1967
SUMMARY— 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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Phenoloxidase of Mycobacterium leprae

Nature, 1967
INVESTIGATIONS 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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Screening for Phenoloxidases from Edible Mushrooms

Bioscience, Biotechnology, and Biochemistry, 2001
A screening test for phenoloxidases from edible mushrooms was done on potato dextrose agar plates that contained phenolic chemicals. Many edible mushrooms showed positive reactions on the agar plates. Among them, Auricularia auricula-judae, Clitocybe nebularis, Lentinus edodes, Pholiota aurivella, and Pseudohiatula oshimae produced a considerable ...
K, Morisaki, T, Fushimi, S, Kaneko, I, Kusakabe, H, Kobayashi   +4 more
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Molecular Forms of Apple Phenoloxidase

Biochemie und Physiologie der Pflanzen, 1979
Summary 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, G.B. Samorodova-Bianki, S.A. Strel'tsina   +2 more
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Processing of crayfish hemocyanin subunits into phenoloxidase

Biochemical and Biophysical Research Communications, 2004
Hemocyanin 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, Bok Luel, Lee, Kenneth, Söderhäll   +2 more
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