High-Voltage Paper Electrophoresis (HVPE) of Cell-Wall Building Blocks and Their Metabolic Precursors

Author(s):  
Stephen C. Fry
1964 ◽  
Vol 42 (11) ◽  
pp. 1553-1559 ◽  
Author(s):  
D. Jušić ◽  
C. Roy ◽  
R. W. Watson

Peptides from partial acid hydrolysates of purified mucopeptide from Aerobacter cloacae NRC 492 were isolated by a combination of high-voltage paper electrophoresis and paper chromatography. Three dipeptides (L-ala.D-glu, D-glu.meso-Dap, and meso-Dap.D-ala), two tripeptides (ala.D-glu.meso-Dap and D-glu.meso-Dap.ala, i.e. D-glutamyl.meso-diaminopimelyl.alanine), and a tetrapeptide were partially characterized. Molar ratios, sequence, and optical configurations in a tripeptide from the wall corresponded with those in a uridine diphospho muramyl tripeptide from penicillin-treated cells of the same organism and with those of a tripeptide synthesized in vitro by enzymes from cell sonicates.


Xenobiotica ◽  
1981 ◽  
Vol 11 (12) ◽  
pp. 841-847 ◽  
Author(s):  
J. A. Bell ◽  
A. Bradbury ◽  
L. E. Martin ◽  
R. J. N. Tanner

1969 ◽  
Vol 22 (5) ◽  
pp. 1197 ◽  
Author(s):  
RL Darskus ◽  
JM Gillespie ◽  
H Lindley

S-Carboxymethyl derivatives of the high-sulphur components of reduced Merino wool have been subdivided by chromatography into 17 fractions, the amino acid compositions of which are reported. Tryptic, chymotryptic, and thermolysin digests of each fraction have been studied by high-voltage paper electrophoresis at pH 3�5 and 6�5. The results suggest that the high-sulphur proteins consist of families of proteins probably containing common structural features. Evidence is presented that the heterogeneity of high-sulphur proteins is not artefactual.


1964 ◽  
Vol 42 (2) ◽  
pp. 219-227 ◽  
Author(s):  
Arthur E. Pasieka

Two major improvements on a high voltage paper electrophoresis apparatus are described. Special tinned brass radiator plates have been very effective for cooling the system. Multichambered electrolyte vessels have facilitated the separation of various biological mixtures at several pH's in a single run at room temperature.


2020 ◽  
Vol 86 (7) ◽  
Author(s):  
Isaac Cann ◽  
Gabriel V. Pereira ◽  
Ahmed M. Abdel-Hamid ◽  
Heejin Kim ◽  
Daniel Wefers ◽  
...  

ABSTRACT Renewable fuels have gained importance as the world moves toward diversifying its energy portfolio. A critical step in the biomass-to-bioenergy initiative is deconstruction of plant cell wall polysaccharides to their unit sugars for subsequent fermentation to fuels. To acquire carbon and energy for their metabolic processes, diverse microorganisms have evolved genes encoding enzymes that depolymerize polysaccharides to their carbon/energy-rich building blocks. The microbial enzymes mostly target the energy present in cellulose, hemicellulose, and pectin, three major forms of energy storage in plants. In the effort to develop bioenergy as an alternative to fossil fuel, a common strategy is to harness microbial enzymes to hydrolyze cellulose to glucose for fermentation to fuels. However, the conversion of plant biomass to renewable fuels will require both cellulose and hemicellulose, the two largest components of the plant cell wall, as feedstock to improve economic feasibility. Here, we explore the enzymes and strategies evolved by two well-studied bacteria to depolymerize the hemicelluloses xylan/arabinoxylan and mannan. The sets of enzymes, in addition to their applications in biofuels and value-added chemical production, have utility in animal feed enzymes, a rapidly developing industry with potential to minimize adverse impacts of animal agriculture on the environment.


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