Protein electrophoretic

FIG. 6 Comparison of protein electrophoretic mobility ratios as functions of protein molecular weight for SDS-templated gels of various compositions (data points) to Fergnson plots of reference normal gels. (Reprinted by permission of Wiley-VCH from Ref. 322, Copyright 1996, Wiley-VCH.)... 

Hirose I et al. Proteome analysis of Bacillus subtilis extracellular proteins a two-dimensional protein electrophoretic study. Microbiology 2000 146 65-75. 

His method was used by Longsworth Machines (Ref 2) for analysis of proteins. Electrophoretic analysis was also used by Svensson (Ref 4) and was described in the book of Weissberger (Ref 5). 

Marchal, R., Berthier, L., Legendre, L., Marchal-Delahaut, P., Jeandet, P., and Maujean, A. (1998). Effects of Botrytis cinerea infection on the must protein electrophoretic characteristics. J. Agric. Food Chem. 46,4945 4949. 

Protein Electrophoretic Mobility Subunit Weight (kdal)... 

In addition to staining for total protein, electrophoretic gels can be used for detection of specific protein components. This can be done, for example, by treating the gel in conditions suitable to reveal enzymatic activities, such as chitinolytic (Vincenzi and Curioni, 2005), or staining for glycoproteins with the periodic acid-Schiff method (PAS) (e.g. Marchal et ah, 1996). 

Serum protein electrophoretic patterns. [Pattern (a) i.s reproduced, with permission, from Helena Laboratories, Beaumont, Texas.]... 

A PDMS microfluidic system has been reported by Dodge and coworkers [135] that combined on-line protein electrophoretic separation, selection, and digestion of... 

Proteins can ba fractionated by electrophoretic techniques on the basis of one or a combination of their three major properties size, net charge and relative hydrophobicity. Electrophoresis under native conditions is ideal for soluble proteins, where biological properties can often be retained. In contrast, more vigorous and often denaturing conditions must be used for analysis of less soluble proteins. Electrophoretic separations can be carried out using either a continuous or discontinuous (Multiphasic) buffer system. The techniques are referred to as continuous zone electrophoresis (CZE) or discontinuous ("disc") electrophoresis (also known as multiphasic zone electrophoresis, MZE). 

AUchin, J. P, and G. O. Evans. 1986. Serum protein electrophoretic patterns of the marmoset, Callithrix jacchus. Journal of Comparative Pathology 96 349-352. 

Electrophoresis, a process of separating compounds on the basis of their electric charges, is used to separate and identify mixtures of amino acids and proteins. Electrophoretic separations can be carried out with paper, starch, agar, certain plastics, and cellulose acetate used as solid supports. In paper electrophoresis, a paper strip saturated with an aqueous buffer of predetermined pH serves as a bridge between two electrode vessels (Figure 18.4). Next, a sample of amino acids is applied as a colorless spot on the paper strip. (The amino acid... 

Assemble the transfer sandwich Scotch Brite pad (or equivalent scouring pad), three layers of Whatman 3MM paper, the gel, the membrane (nitrocellulose, nylon, or Immobilon-P—the latter has to be prewetted in methanol), three layers of 3MM paper, and another Scotch Brite pad. Transfer gel-fractionated proteins electrophoretically to a membrane under conditions that have been experimentally determined to be best for the protein of interest. With a Bio-Rad Trans-Blot apparatus, transfer of a 60-kDa protein can be accompUshed using 60 V for 1 hr. 

The mucin precipitated from synovial fluids by weak acids appears to be a dissociable complex of hyaluronic acid and proteins. Electrophoretic studies of synovial fluids (at pH 8.6) have usually shown the presence of one fast-moving component considered to be free hyaluronic acid, but some fluids show a second fast component, possibly a hyaluronic acid -- protein complex (69). On the basis of studies in the ultracentrifuge, the mucin possibly may exist in synovial fluid partially as a mucoprotein with a molecular weight of one to ten million (70). Electrophoretic and ultracentrifugal measurements at varying pH values provide two of the best ways of demonstrating interaction in such systems. 

Multi-variable or cold-ethanol precipitation techniques yielded plasma protein fractions rich in lipoprotein (Oncley et al. 1949). These isolation procedures were extremely important. They demonstrated that physical properties such as solubility could be studied with lipoproteins as well as other proteins. Electrophoretic mobilities and specific refractive increments of lipoproteins were shown to be measurable properties (Armstrong et al. 1947 a and 1947 b). A detailed analysis of lipoprotein composition was undertaken (Oncley et al. 1950). 

Where [L] is ligand concentration, [P] is concentration of sample protein, Rq and r protein electrophoretic mobility in the absence and the presence of ligand. Obtained dissociation constant is apparent dissociation constant in gel, and may be different from dissociation constant in solution. 

One of the highest 2,3-BD yields was reported from Bacillus licheniformis. The theoretical yield of 2,3-BD fi-om glucose is 0.5 g/g of glucose. Bacillus licheniformis was able to reach 94 % of the theoretical yield in 72 h. The best yields were obtained when peptone and beef extract were added to the medium. This productivity was similar to that of Klebsiella and Bacillus polymyxa (Nilegaonkar et al. 1992). Additional work to characterize B. licheniformis strains was done by using profiles of the fermentation products formed. A number of B. licheniformis strains were compared with B. polymyxa strains. The product profiles for the B. licheniformis strains were similar to each other however, they differed from the B. polymyxa strains. Protein electrophoretic patterns were also used to classify the strains. Again, with protein electrophoretic patterns, B. licheniformis was mapped in a different cluster than B. polymyxa. In fermentation tests, some of the B. licheniformis strains were shown to be as promising as B. polymyxa for 2,3-BD production (Raspoet et al. 1991). 

Fig. 28. Protein electrophoretic pattern of unfractionated chloroplast membranes from C. rein-hardi y-1 and of fractions produced by Triton X-lOO treatment. Electrophoresis was carried out by the phenol-acetic acid method." Fraction 2 consists of PSII particles and is highly enriched in a main peak (3 cm from the origin) identical with the L protein. Fraction 3 consists of PSI particles and is relatively poor in this protein. (For experimental details see ref. 81.)...

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