Reptation mechanism in protein–sodium-dodecylsulfate (SDS) polyacrylamide-gel electrophoresis

Guo, Xuan-Hui; Chen, Sow‐Hsin

doi:10.1103/physrevlett.64.2579

Cited by 22 publications

(18 citation statements)

References 19 publications

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“…Among the possible separation polymer matrices, different chain length polyethylene oxides (PEO) have recently been successfully utilized as replaceable sieving media [ l l , 12, 14, 181. Compared to the most commonly used electrophoretic DNA separation methods, such as polyacrylamide and agarose gel electrophoresis [ 19,201, the separation mechanism in SDS-gel electrophoresis has not been thoroughly investigated yet. Few papers discuss the actual migration behavior and separation principles of the SDSprotein complexes during gel electrophoresis [21,221. Early publications of SDS-PAGE-based separations often applied the so-called Ogston sieving model to describe the migration process of the SDS-protein complexes through a crosslinked polymer matrix with a given pore size [4, 51.…”

Section: Introductionmentioning

confidence: 99%

“…This suggests that the conventional Ogston model is not always appropriate to explain the migration mode of relatively large species through a small pore size sieving matrix. It was speculated that protein-SDS complexes may undergo reptation-like motion during the SDS-PAGE process in the polymer network [21].…”

Section: Introductionmentioning

confidence: 99%

“…This value is much smaller than the contour lengths of the majority of protein-SDS complexes. Guo and Chen [21] studied the structure of SDS-BSA complex (contour length -100 nm) and fit their data to the so-called "necklace model" [25]. This model assumes that the unfolded polypeptide chain is flexible in solution, and micelle-like clusters of SDS molecules are formed along the polypeptide backbone.…”

Section: Introductionmentioning

confidence: 99%

“…However, the Ogston model cannot be used in all instances to explain mobility differences. One of the reasons is that the pore size of the polyacrylamide gels commonly employed in most of the slab gel separations is in the range of several nanometers [5, 21,23,241. This value is much smaller than the contour lengths of the majority of protein-SDS complexes.…”

Section: Introductionmentioning

confidence: 99%

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On the separation mechanism of capillary sodium dodecyl sulfate‐gel electrophoresis of proteins

Guttman¹

1995

Electrophoresis

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Polyethylene oxide-mediated capillary sodium dodecyl sulfate-electrophoresis is a recently established, high-resolution separation method for fast purity check and molecular mass assessment of protein molecules. The effects of the sieving polymer chain length and concentration on the separation mechanism of sodium dodecyl sulfate-protein complexes were examined. The studies aimed to clarify whether the separation can be described by either the Ogston sieving theory, or the reptation or reptation-with-stretching theory. Polyethylene oxides with molecular masses of 100,000, 300,000 and 900,000 Da were used as separation matrices at various concentrations ranging from 1-4%, 0.5-2% and 0.25-1%, respectively. The separation phenomena was examined using a standard protein test mixture containing six proteins in the molecular mass range of 14,200-97,400 Da. A possible separation mechanism of reptation with stretching is suggested, where separation performance was improved with increasing sieving polymer chain lengths and/or concentration.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

On the separation mechanism of capillary sodium dodecyl sulfate‐gel electrophoresis of proteins

Guttman¹

1995

Electrophoresis

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“…3) suggests that in the molecular weight range examined, the k exponent is approximately -0.2. Note that in slab gel electrophoresis this exponent is --1 [14] under isoterm and isoelectrostatic (constant field strength) conditions. the migration velocity increased with elevated temperature.…”

Section: By Combining Eqs (1)-(3)mentioning

confidence: 99%

Effect of operational variables on the separation of proteins by capillary sodium dodecyl sulfate‐gel electrophoresis

Guttman¹,

Shieh²,

Hoang³

et al. 1994

Electrophoresis

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Capillary sodium dodecyl sulfate (SDS)-gel electrophoresis, for fast and high-resolution separations of protein molecules based on their molecular masses was investigated, employing a polymeric sieving network of polyethylene oxide (PEO). A standard mixture of five proteins ranging from 14.2-66.0 kDa in molecular mass was used to evaluate the sieving matrix. A general migration velocity equation was derived for capillary SDS-gel electrophoresis of proteins and supported by the experimental data. This equation gives a better understanding of SDS-protein separations via capillary gel electrophoresis. Results are presented regarding the effects of different operational variables such as gel concentration, electric field strength, molecular mass, and temperature on the electrophoretic migration properties of the different size protein molecules.

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Observation of orientation and relaxation of protein‐sodium dodecyl sulfate complexes during pulsed intermittent field polyacrylamide gel electrophoresis

1991

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Polyacrylamide gel electrophoresis (PAGE) of proteins denatured with SDS (sodium dodecyl sulfate) has been used successfully to separate proteins according to their molecular mass. In spite of the extensive use of this technique, the motion of the protein-SDS complex in a polyacrylamide gel is still not understood. Here we report on the observation of the orientation (in the field direction) and relaxation of protein-SDS complexes during pulsed intermittent field PAGE experiments. The results give an indication of the stiffness of the molecules and may be useful for the development of a technique to improve the separation of large proteins using pulsed electric fields.

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Reptation mechanism in protein–sodium-dodecylsulfate (SDS) polyacrylamide-gel electrophoresis

Cited by 22 publications

References 19 publications

On the separation mechanism of capillary sodium dodecyl sulfate‐gel electrophoresis of proteins

On the separation mechanism of capillary sodium dodecyl sulfate‐gel electrophoresis of proteins

Effect of operational variables on the separation of proteins by capillary sodium dodecyl sulfate‐gel electrophoresis

Observation of orientation and relaxation of protein‐sodium dodecyl sulfate complexes during pulsed intermittent field polyacrylamide gel electrophoresis

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