Association of sulfhydryl oxidase and xanthine oxidase in bovine mammary tissue

The presence of antigenically active xanthine oxidase was indicated in various relatively purified preparations of sulfhydryl oxidase obtained from bovine milk. Evidence for formation of a complex of the two enzymes was obtained by double immunodiffusion. Furthermore, sodium dodecylsulfate-gel elect...

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Bibliographic Details
Published in:Journal of dairy science 1986-11, Vol.69 (11), p.2803-2809
Main Authors: Blakistone, B.A, Aurand, L.W, Swaisgood, H.E
Format: Article
Language:English
Subjects:
Animals
Cattle
CELL STRUCTURE
Electrophoresis
ESTABILIDAD
ESTRUCTURA CELULAR
Female
GLANDE MAMMAIRE
GLANDULAS MAMARIAS
GRASA DE LA LECHE
LAIT
LECHE
MAMMARY GLANDS
Mammary Glands, Animal - analysis
Mammary Glands, Animal - enzymology
MATIERE GRASSE DU LAIT
MILK
Milk - enzymology
MILK FAT
OXIDACION
OXIDATION
OXIDOREDUCTASES
Oxidoreductases - analysis
Oxidoreductases - metabolism
OXIDORREDUCTASAS
OXYDATION
OXYDOREDUCTASE
STABILITE
STABILITY
STRUCTURE CELLULAIRE
THIOL
THIOLS
TIOLES
Xanthine Oxidase - analysis
Xanthine Oxidase - metabolism
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Summary:The presence of antigenically active xanthine oxidase was indicated in various relatively purified preparations of sulfhydryl oxidase obtained from bovine milk. Evidence for formation of a complex of the two enzymes was obtained by double immunodiffusion. Furthermore, sodium dodecylsulfate-gel electrophoresis of sulfhydryl oxidase and xanthine oxidase model mixtures indicated that high molecular weight species were present that reacted with both antisulfhydryl oxidase and antixanthine oxidase. Similar gel electrophoretic patterns visualized by protein-dye binding methods revealed a distinct band (greater than 200 kdalton) was formed upon incubation of mixtures of the two enzymes, the presence of which was unaffected by reduction of protein disulfide bonds. Immunofluorescent staining techniques showed both enzymes in the apical plasma membrane. Because sulfhydryl oxidase previously has been shown to catalyze conversion of the dehydrogenase form of xanthine oxidase to the oxidase form, this conversion may occur when xanthine oxidase contacts sulfhydryl oxidase in the apical plasma membrane. This conversion and the resulting potential for production of active oxygen species could be significant to membranotropic processes, such as fat globule secretion, and to the oxidative stability of the milk fat globule membrane.
ISSN:0022-0302
1525-3198
DOI:10.3168/jds.S0022-0302(86)80733-0