Isolation of ?-(1?4)-glucan synthetase from cottonplant shoots

1994 ◽  
Vol 30 (1) ◽  
pp. 78-80
Author(s):  
A. A. Akhunov ◽  
F. A. Ibragimov ◽  
�. Ch. Mustakimova
Keyword(s):  
Glucan Synthetase

scholarly journals Interaction between yeast beta-(1 goes to 3)glucan synthetase and activating phosphorylated compounds. A kinetic study.

1982 ◽  
Vol 257 (4) ◽  
pp. 1902-1905
Author(s):  
V. Notario ◽  
H. Kawai ◽  
E. Cabib
Keyword(s):  
Kinetic Study ◽  
Phosphorylated Compounds ◽  
Glucan Synthetase

Purification par séparation de phase et caractérisation du plasmalemme de l'épicotyle de pois

1986 ◽  
Vol 64 (5) ◽  
pp. 448-455 ◽  
Author(s):  
Jacques Rembur ◽  
Pierre Landré ◽  
Arlette Nougarède
Keyword(s):  
Atpase Activity ◽  
Plasma Membranes ◽  
Microsomal Fraction ◽  
Alkaline Ph ◽  
Phase Partition ◽  
Pea Epicotyl ◽  
Glucan Synthetase ◽  
Triton X ◽  
Two Sides ◽  
Slight Contamination

The validity of phase partition to obtain a substantial proportion of vesicles of plasmalemma origin from the microsomal fraction of pea epicotyl has been demonstrated. In the fractions enriched with plasma membranes, N-naphthyl phtalamic acid binding and β-glucan synthetase II activity, showed a yield of about 60% and an enrichment of 2.3 and 2.2, respectively, in comparison with the microsomal fraction. When such plasmalemmic vesicles are permabilized by Triton X-100, an intense Mg2+-ATPase activity is obtained in presence of K+ at acid as well as alkaline pH. Inhibition of Mg2+-ATPase by vanadate in presence of K+ and its variations in relation to pH were shown. Dicyclohexylcarbodiimide and diethylstilbestrol inhibit 40–55% of this enzymatic activity, both at acid and neutral pH. The data show a slight contamination of the plasmalemmic fraction by endomembranes and suggest an asymmetry of the two sides of the plasmalemma.

Particulate glucan synthetase activity: Generation and inactivation after treatments with indoleacetic acid and cycloheximide

1972 ◽  
Vol 152 (1) ◽  
pp. 311-317 ◽  
Author(s):  
F.S. Spencer ◽  
G. Shore ◽  
B. Ziola ◽  
G.A. Maclachlan
Keyword(s):  
Indoleacetic Acid ◽  
Synthetase Activity ◽  
Activity Generation ◽  
Glucan Synthetase

Multiple forms of α-1,4 glucan synthetase from spinach leaves

1971 ◽  
Vol 43 (3) ◽  
pp. 631-636 ◽  
Author(s):  
J.L. Ozbun ◽  
J.S. Hawker ◽  
Jack Preiss
Keyword(s):  
Multiple Forms ◽  
Glucan Synthetase ◽  
Spinach Leaves

Lipids and Enzymatic Activities in Vacuolar Membranes Isolated via Protoplasts from Oat Primary Leaves

1983 ◽  
Vol 38 (9-10) ◽  
pp. 770-777 ◽  
Author(s):  
Britta Verhoek ◽  
Renate Haas ◽  
Käthe Wrage ◽  
Michael Linscheid ◽  
Ernst Heinz
Keyword(s):  
Membrane System ◽  
Enzymatic Activities ◽  
Membrane Preparation ◽  
Chloroplast Envelope ◽  
Mesophyll Protoplasts ◽  
Golgi Membranes ◽  
Significant Contamination ◽  
Nadh Cytochrome ◽  
Glucan Synthetase ◽  
Vacuolar Membranes

Vacuoles were released from oat (Avena sativa) mesophyll protoplasts and purified by sedi­mentation and flotation. Disruption of isolated vacuoles followed by density gradient centri­fugation gave two membrane bands which after combination were further purified on sucrose gradients. A significant contamination by microbodies, thylakoids, mitochondria, endoplasmic reticulum and Golgi membranes can be excluded, whereas markers for plasma membrane and chloroplast envelope were present in the final membrane preparation.In the purified membrane fraction the following enzymatic activities were detected: NADH- cytochrome C reductase E.C. 1.6.2.2, ATPase E.C. 3.6.1.3. UDPG: sterol glucosyltransferase, UDP-Gal: diacylglycerol galactosyltransferase E.C. 2.4.1.46, glucan synthetase II, CDP-choline: diacylglycerol phosphocholinetransferase E.C. 2.7.8.2, formation of acylgalactosyl diacylglycerol and acyl-CoA thioesterase E.C. 3.1.2.2. None of these can be considered to be specific for the tonoplast. Acid phosphatase E.C. 3.1.3.2 was present in the cell sap.The vacuolar membranes contain phospholipids and glycolipids of the most complex composi­tion found so far in a membrane system isolated from mesophyll protoplasts. About half of the glycolipids were accounted for by glycosyl diacylglycerols usually considered to be confined to plastids. Steryl glycosides and acyl steryl glycosides were other prominent glycolipids. A cerebroside was the predominating lipid component of this membrane preparation.

Properties of ?-glucan synthetase from Saccharomyces cerevisiae

1978 ◽  
Vol 44 (3-4) ◽  
pp. 329-339 ◽  
Author(s):  
E. L�pez-Romero ◽  
J. Ruiz-Herrera
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Glucan Synthetase

scholarly journals Molecular Cloning and Characterization of cgs, theBrucella abortus Cyclic β(1-2) Glucan Synthetase Gene: Genetic Complementation of Rhizobium meliloti ndvB andAgrobacterium tumefaciens chvB Mutants

1998 ◽  
Vol 180 (17) ◽  
pp. 4392-4400 ◽  
Author(s):  
Nora Iñón de Iannino ◽  
Gabriel Briones ◽  
Marcelo Tolmasky ◽  
Rodolfo A. Ugalde
Keyword(s):  
Amino Acids ◽  
Membrane Protein ◽  
Rhizobium Meliloti ◽  
Nodule Development ◽  
Nucleotide Sequencing ◽  
Insertion Mutant ◽  
Reading Frame ◽  
Glucan Synthesis ◽  
Glucan Synthetase

ABSTRACT The animal pathogen Brucella abortus contains a gene,cgs, that complemented a Rhizobium melilotinodule development (ndvB) mutant and an Agrobacterium tumefaciens chromosomal virulence (chvB) mutant. The complemented strains recovered the synthesis of cyclic β(1-2) glucan, motility, virulence in A. tumefaciens, and nitrogen fixation in R. meliloti; all traits were strictly associated with the presence of an active cyclic β(1-2) glucan synthetase protein in the membranes. Nucleotide sequencing revealed the presence in B. abortus of an 8.49-kb open reading frame coding for a predicted membrane protein of 2,831 amino acids (316.2 kDa) and with 51% identity to R. meliloti NdvB. Four regions of the B. abortus protein spanning amino acids 520 to 800, 1025 to 1124, 1284 to 1526, and 2400 to 2660 displayed similarities of higher than 80% with R. meliloti NdvB. Tn3-HoHo1 mutagenesis showed that the C-terminal 825 amino acids of the Brucella protein, although highly conserved inRhizobium, are not necessary for cyclic β(1-2) glucan synthesis. Confirmation of the identity of this protein as B. abortus cyclic β(1-2) glucan synthetase was done by the construction of a B. abortus Tn3-HoHo1 insertion mutant that does not form cyclic β(1-2) glucan and lacks the 316.2-kDa membrane protein. The recovery of this mutant from the spleens of inoculated mice was decreased by 3 orders of magnitude compared with that of the parental strain; this result suggests that cyclic β(1-2) glucan may be a virulence factor inBrucella infection.

scholarly journals Mechanism of action of cyclic beta-1,2-glucan synthetase from Agrobacterium tumefaciens: competition between cyclization and elongation reactions.

1992 ◽  
Vol 174 (24) ◽  
pp. 7941-7947 ◽  
Author(s):  
G Williamson ◽  
K Damani ◽  
P Devenney ◽  
C B Faulds ◽  
V J Morris ◽  
...  
Keyword(s):  
Agrobacterium Tumefaciens ◽  
Mechanism Of Action ◽  
Glucan Synthetase

scholarly journals Nucleotide Sequencing and Transcriptional Analysis of Two Tandem Genes Encoding Glucosyltransferase (Water-Soluble-Glucan Synthetase) inStreptococcus cricetusHS-6

2000 ◽  
Vol 44 (9) ◽  
pp. 755-764 ◽  
Author(s):  
Miho Inoue ◽  
Tetsuyoshi Inoue ◽  
Atsushi Miyagi ◽  
Ichiro Tanimoto ◽  
Ryuji Shingaki ◽  
...  
Keyword(s):  
Water Soluble ◽  
Transcriptional Analysis ◽  
Nucleotide Sequencing ◽  
Genes Encoding ◽  
Tandem Genes ◽  
Glucan Synthetase
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