Results 181 to 190 of about 6,311 (212)
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Mode of Action of Glycogen Branching Enzyme from Neurospora crassa
The Journal of Biochemistry, 1990Neurospora crassa branching enzyme [EC 2.4.1.18] acted on potato amylopectin or amylose to convert them to highly branched glycogen-type molecules which consisted of unit chains of six glucose units. The enzyme also acted on the amylopectin beta-limit dextrin, indicating that the enzyme acted on internal glucose chains as well as outer chains.
A, Matsumoto, T, Nakajima, K, Matsuda
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Biosynthesis of Glycogen in Neurospora crassa. Purification and Properties of the Branching Enzyme
The Journal of Biochemistry, 1983A branching enzyme was extracted from the mycelia of Neurospora crassa and was purified to electrophoretic homogeneity by procedures including DEAE-Sephacel column chromatography, 6-aminohexyl-Sepharose 4B column chromatography and gel filtration on Toyopearl HW-55S.
A, Matsumoto, T, Kamata, K, Matsuda
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Apparent absence of glycogen branching enzyme activity in phosphofructokinase deficiency
Journal of Inherited Metabolic Disease, 1991SummaryA 30‐year‐old woman with clinical features and biochemical findings of muscle phosphofructokinase deficiency was found to have a very low level of α‐1,4‐glucan:α‐1,4‐glucan‐6‐transglucosylase (branching enzyme, EC 2.4.1.18) activity in muscle. In contrast, branching enzyme activity in the leukocytes was in the range of control values.
V, Barash +3 more
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Glycogen brain branching enzyme.
Cellular and molecular biology (Noisy-le-Grand, France), 1998Rat brain glycogen branching enzyme was partially purified in order to elucidate its mechanism of action. The alpha1,4-alpha1,6-glucan polysaccharide was synthesized using rat brain branching enzyme under two different elongation conditions: Glc-1-P and phosphorylase or UDP-Glc and glycogen synthase.
D S, Tolmasky, C, Labriola, C R, Krisman
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Journal of Pediatrics, 2004
The fatal neonatal form of type IV glycogen storage disease (GSD IV) was diagnosed on light and electron microscopy and by analysis of GBE1 , the gene encoding glycogen branching enzyme. We report two novel truncating mutations, as well as the first genomic mutational analysis of GBE1 using denaturing high performance liquid chromatography.
Andreas R Janecke
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The fatal neonatal form of type IV glycogen storage disease (GSD IV) was diagnosed on light and electron microscopy and by analysis of GBE1 , the gene encoding glycogen branching enzyme. We report two novel truncating mutations, as well as the first genomic mutational analysis of GBE1 using denaturing high performance liquid chromatography.
Andreas R Janecke
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Glycogen branching enzyme (GBE1) mutation causing equine glycogen storage disease IV
Mammalian Genome, 2004Comparative biochemical and histopathological evidence suggests that a deficiency in the glycogen branching enzyme, encoded by the GBE1 gene, is responsible for a recently identified recessive fatal fetal and neonatal glycogen storage disease (GSD) in American Quarter Horses termed GSD IV.
Ward, T. +5 more
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Preparation of branched starch by α-amylase and thermophilic glycogen branching enzyme modification
Food ChemistryMaltogenic α-amylase (MA, EC 3.2.1.133), which shows high thermal stability, can cleave long starch chains linked by α-1,4 glycosidic bonds. And glycogen branching enzyme (GBE, EC 2.4.1.18) can increase the branching degree of starch. At high temperatures, Elevated temperatures enhanced starch solubilization, improving the accessibility of both MA and ...
Jing, Zhu +8 more
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Glycogen Synthetase (and Branching Enzyme)
1975The second enzyme capable of the synthesis of α-1,4 linkages of glycogen is glycogen synthetase*. Unlike phosphorylase, it is synthetic both in vitro and in vivo, it seems to have similar properties in all tissues including CNS, and can not degrade glycogen; it is now proved to be the only synthetic enzyme under normal in vivo conditions.
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International Journal of Biological Macromolecules
In practical applications, the gelatinisation temperature of starch is high. Most current glycogen branching enzymes (GBEs, EC 2.4.1.18) exhibit optimum activity at moderate or low temperatures and quickly lose their activity at higher temperatures, limiting the application of GBEs in starch modification.
Jie Long, Xingfei Li, Chao Qiu
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In practical applications, the gelatinisation temperature of starch is high. Most current glycogen branching enzymes (GBEs, EC 2.4.1.18) exhibit optimum activity at moderate or low temperatures and quickly lose their activity at higher temperatures, limiting the application of GBEs in starch modification.
Jie Long, Xingfei Li, Chao Qiu
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Food Research International
Starch plays a vital role in societal development. However, during industrial processing, the properties and structure of starch change considerably, leading to limitations in its application. Starches need to be modified to meet industrial demand. Glycogen branching enzymes (GBEs) are important tools for the branched modification of starch, which ...
Jing, Zhu +8 more
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Starch plays a vital role in societal development. However, during industrial processing, the properties and structure of starch change considerably, leading to limitations in its application. Starches need to be modified to meet industrial demand. Glycogen branching enzymes (GBEs) are important tools for the branched modification of starch, which ...
Jing, Zhu +8 more
openaire +2 more sources