منابع مشابه
Hydrogen peroxide-dependent conversion of nitrite to nitrate as a crucial feature of bovine milk catalase.
The enzyme catalase is well-known to catalyze the disintegration of hydrogen peroxide to water and oxygen; however, this study shows that its main function in bovine milk is oxidation of nitrite to nitrate. This process depends on hydrogen peroxide, of which the main source appears to be hydrogen peroxide formation that is coupled to the conversion of purines--xanthine in the present study--to ...
متن کاملTurnover of genetically defined catalase isozymes in maize.
The turnover of two homotetramers of catalase, V(4) and Z(4), specified by genes at two separate loci, has been studied during germination of maize seed by the techniques of density labeling and starch-gel electrophoresis. Both isozymes were shown to be turning over during this time. However, Z(4) accumulates because the rate of synthesis exceeds the rate of degradation, whereas V(4) slowly dis...
متن کاملIsozymes of bovine intestinal alkaline phosphatase.
Alkaline phosphatases from calf and bovine small intestines have been isolated in homogeneous form from both mucosa and luminal contents. The detergent-solubilized calf enzyme resolves into two peaks of activity, C-1 and C-2, on chromatofocusing. Only one of these activity peaks is present in the enzyme from the adult animal. Amino acid compositions, N-terminal sequences, and tryptic peptide ma...
متن کاملBovine milk glycome.
Bovine milk oligosaccharides have several potentially important biological activities including the prevention of pathogen binding to the intestinal epithelial and as nutrients for beneficial bacteria. It has been suggested that milk oligosaccharides are an important source of complex carbohydrates as supplements for the food and the pharmaceutical industries. However, only a small number of st...
متن کاملRibonuclease in Bovine Milk
The RNase (EC 2.7.7.16) in bovine milk was partially purified from milk whey. The basic properties and the hydrolyzing specificity of this enzyme were studied. This enzyme was heat stable. When RNA was used as the substrate, the pH optimum was 7.5 and 3'nucleotides were produced, but the extent of the hydrolysis stopped at 31 per cent and core was left. C! and U! were hydrolyzed but purine cycl...
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ژورنال
عنوان ژورنال: Journal of Dairy Science
سال: 1983
ISSN: 0022-0302
DOI: 10.3168/jds.s0022-0302(83)82113-4