Glycogen brain branching enzyme.
Rat 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. The products obtained demonstrated that the cpolysaccharides synthesized (pattern of the spectra obtained in the presence of Krisman's reagent, lambda max, parameter A and R, % beta-amylolysis and degree of branching) under different incubation times are nearly constant. These results imply that the degree of branching of a polysaccharide depends only on the enzyme specificity.
Tolmasky
D S
DS
Instituto de Investigaciones Bioquímicas Luis F. Leloir Fundación Campomar, Consejo Nacional de Investigaciones Científicas y Técnicas, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Argentina.
Labriola
C
C
Krisman
C R
CR
D015061:1,4-alpha-Glucan Branching Enzyme / Q000378:metabolism*; D000042:Absorption; D000818:Animals; D001921:Brain / Q000201:enzymology*; D005958:Glucosephosphates / Q000378:metabolism; D006005:Phosphorylases / Q000378:metabolism; D011134:Polysaccharides / Q000096:biosynthesis; D051381:Rats; D017208:Rats, Wistar; D001614:beta-Amylase / Q000378:metabolism
D005958:Glucosephosphates; D011134:Polysaccharides; C031590:glucose-1-phosphate; D006005:Phosphorylases; D015061:1,4-alpha-Glucan Branching Enzyme; D001614:beta-Amylase