Relative electrophoretic mobility

FIGURE 5A.4 A plot of the relative electrophoretic mobility of proteins in SDS-PAGE versns the log of the molecnlar weights of the individnal polypeptides. 

In CZE, separations are controlled by differences in the relative electrophoretic mobilities of the individual components in the sample or test solution. The mobility differences are functions of analyte charge and size under specific method conditions. They are optimized by appropriate control of the composition of the buffer, its pH, and its ionic strength. 

Several of the minor proteins of the MFGM have been isolated and partially characterized (Keenan and Dylewski, 1995). A systematic nomenclature has not been developed for the MFGM proteins and most are referred to by their relative electrophoretic mobility on SDS-PAGE and whether or not they are glycoproteins. The proteins of the MFGM represent approximately 1 % of the total proteins in milk. 

The ADSA Protein Nomenclature Committee (Eigel et al. 1984) recommends that these minor K-caseins be identified temporarily according to their genetic variant and numbered consecutively in their order of increasing relative electrophoretic mobility in alkaline urea gels in the presence of mercaptoethanol (Yaguchi et al 1968) as K-casein A-l or K-casein B-l, etc. 

What assumption is made about the relative electrophoretic mobility of bromophenol blue dye and plasmid DNA ... 

Its relative electrophoretic mobility in denaturing and non-denaturing polyacrylamide gels indicated that it had a dimeric structure with an estimated molecular mass of 65kDa per monomer (Figure 11.1). This was confirmed by... 

Size estimate. The relative electrophoretic mobilities of a 30-kd protein and a 92-kd protein used as standards on an SDS-polyacrylamide gel are 0.80 and 0.41, respectively. What is the apparent mass of a protein having a mobility of 0.62 on this gel ... 

What are the relative electrophoretic mobilities of glycine, leucine, aspartic acid, glutamic acid, and lysine at pH 4.70 ... 

What are the relative electrophoretic mobilities at pH 5.68 of the five amino acids given in problem 1 ... 

P2. Parsons, R. S., and Polya, J. B., Relative electrophoretic mobilities of some constituents of human serum. Emymologia 26, 269-280 (1963). 

Figure 5. Relative electrophoretic mobility of esterases involved in organophosphate insecticide resistance in Culex mosquitoes.

Figure 24. Change in relative electrophoretic mobility (pRc,) due to number of modified nucleotides in 12-mer (3 -dA Y]-A(x]PEG-5 ) [x] = number of modifications. PEG = 2 -0-(3,6,9,12,15-pentaoxahexad-ecyl). From [149].

Fig. 3-3. Relative electrophoretic mobility of some hemoglobins (paper electrophoresis, pH 8.6 veronal buffer)...

The electrophoretic mobility of a peptide, determined relative to the EOF or to a standard, can be used for identification. Because at pH 2.5 the EOF is virtually suppressed and difficult to determine experimentally, (26) the relative electrophoretic mobilities of the nine peptides were determined using an internal standard, Dynorphin A fragment 1-13. The apparent mobility (p pp) of the reference peptide Dynorphin was found to be 3.05 x 10" ( Dyn== L x L/1 x V Ld=40 cm, Lt=47 cm, t=274.26 sec, V= 22500 Volts). For each peptide the apparent electrophoretic mobility was then determined experimentally and an electrophoretic mobility relative to the reference peptide calculated ( Tt = l app Poyn ) These values are given in Table 1. 

Tris-glycine (pH 8.5) was used as the running buffer for Hk, Mpi, and Pgi. Tris-malate (pH 7.8) was used as the running buffer for 6Pgd (see Richardson et al. (1986) for buffer recipes). Enzyme stains were modified from Hebert and Beaton (1989). Numerous side-by-side comparisons of electromorphs were made to confirm relative electrophoretic mobilities alleles were assigned letter codes with A representing the... 

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