نتایج جستجو برای: galacto

تعداد نتایج: 623  

Journal: :The Biochemical journal 1983
H B Dixon A Cornish-Bowden

We write on behalf of the Nomenclature Committee of the International Union of Biochemistry to comment on the proposal by Scott et al. (1982) to change the name of neuraminic acid to amino-sialosonic acid as a consequence of allotting the name sialose to a hypothetical 3-deoxynonulose. They further propose symbolizing sialose as Sia, sialosonic acid as SiaA, and aminosialosonic acid as SiaNA. W...

Journal: :Clinical chemistry 1977
G A Mason G K Summer H H Dutton R C Schwaner

In galactosemia, prevention of mental retardation depends on early recognition of the disorder and institution of dietary restriction of galactose. We describe an automated fluorometric micromethod for galactose in whole blood spotted on filter paper. Galactose is oxidized by galactose oxidase to D-galacto-hexadialdose and H2O2 and measured as the highly fluorescent condensation product of homo...

2016
Barbara Geiger Hoang-Minh Nguyen Stefanie Wenig Hoang Anh Nguyen Cindy Lorenz Roman Kittl Geir Mathiesen Vincent G.H. Eijsink Dietmar Haltrich Thu-Ha Nguyen

β-Galactosidase from Streptococcus thermophilus was overexpressed in a food-grade organism, Lactobacillus plantarum WCFS1. Laboratory cultivations yielded 11,000 U of β-galactosidase activity per liter of culture corresponding to approximately 170 mg of enzyme. Crude cell-free enzyme extracts obtained by cell disruption and subsequent removal of cell debris showed high stability and were used f...

Journal: :Advances in nutrition 2012
Motomitsu Kitaoka

Intestinal colonization of bifidobacteria is important for the health of infants. Human milk oligosaccharides (HMO) have been identified as growth factors for bifidobacteria. Recently, a bifidobacterial enzymatic system to metabolize HMO was identified. 1,3-β-Galactosyl-N-acetylhexosamine phosphorylase (GLNBP, EC 2.4.1.211), which catalyzes the reversible phosphorolysis of galacto-N-biose (GNB)...

2013
Jaekoo Lee Inkyung Park Jaiesoon Cho

Partially purified α-galactosidase from Bacillus sp. LX-1 was non-covalently immobilized on a reversibly soluble-insoluble polymer, Eudragit L-100, and an immobilization efficiency of 0.93 was obtained. The optimum pH of the free and immobilized enzyme was 6.5 to 7.0 and 7.0, respectively, while there was no change in optimum temperature between the free and immobilized α-galactosidase. The imm...

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