Match!

The Reliability of Molecular Weight Determinations by Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis

Published on Aug 25, 1969in Journal of Biological Chemistry4.106
Klaus Weber111
Estimated H-index: 111
,
M. J. Osborn36
Estimated H-index: 36
Sources
Abstract
Abstract Forty proteins with polypeptide chains of well characterized molecular weights have been studied by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate following the procedure of Shapiro, Vinuela, and Maizel (Biochem. Biophys. Res. Commun., 28, 815 (1967)). When the electrophoretic mobilities were plotted against the logarithm of the known polypeptide chain molecular weights, a smooth curve was obtained. The results show that the method can be used with great confidence to determine the molecular weights of polypeptide chains for a wide variety of proteins.
  • References (2)
  • Citations (14874)
📖 Papers frequently viewed together
12k Citations
697 Citations
3,484 Citations
78% of Scinapse members use related papers. After signing in, all features are FREE.
References2
Newest
#1Klaus Weber (Harvard University)H-Index: 16
New Structural Model of E. coli Aspartate Transcarbamylase and the Amino-acid Sequence of the Regulatory Polypeptide Chain
176 CitationsSource
#1Arnold L. Shapiro (NYU: New York University)H-Index: 4
#2Eladio Viñuela (NYU: New York University)H-Index: 7
Last. Jacob V. Maizel (Albert Einstein College of Medicine)H-Index: 25
view all 3 authors...
2,812 CitationsSource
Cited By14874
Newest
#1Ran Li (UH: University of Helsinki)
#2Xing Wan (UH: University of Helsinki)H-Index: 3
Last. Per E. J. Saris (UH: University of Helsinki)H-Index: 27
view all 4 authors...
The yeast Saccharomyces boulardii is well known for its probiotic effects such as treating or preventing gastrointestinal diseases. Due to its ability to survive in stomach and intestine, S. boulardii could be applied as a vehicle for producing and delivering bioactive substances of interest to human gut. In this study, we cloned the gene lecC encoding the antilisterial peptide leucocin C from lactic acid bacterium Leuconostoc carnosum in S. boulardii. The constructed S. boulardii strain secrete...
Source
#1Yu-li Wang (CMU: Carnegie Mellon University)H-Index: 67
#2David Li (CMU: Carnegie Mellon University)H-Index: 2
Due to its favorable physical and chemical properties, including chemical inertness, low fouling by biological molecules, high porosity and permeability, optical transparency, and adjustable elasticity, polyacrylamide has found a wide range of biomedical and non-biomedical applications. To further increase its versatility, this communication describes a simple method, using readily available reagents and equipment, for 3D printing polyacrylamide hydrogels at a resolution of 100-150 μm to create ...
Source
Gender sensitivity to ambient heat, despite well known in insect species, how it manifests during young and late larval instars of Bombyx mori is still unclear. To uncover this cryptic feature, different instars male and female larvae were subjected to varied thermal stress separately and sex-stage specific expression of proteins was investigated. Interestingly, heat shock proteins (HSPs) 90 and 70 were expressed differently in all the instars and also between male and female larvae as confirmed...
Source
#1Shugo WatabeH-Index: 42
#2Daisuke IkedaH-Index: 6
Last. Mitsuru JimboH-Index: 13
view all 15 authors...
Source
#1Yasser Elbahloul (Taibah University)H-Index: 6
#2Alexander Steinbüchel (KAU: King Abdulaziz University)H-Index: 85
Abstract Until now, no enzymes were described that hydrolyze cyanophycin granular protein (CGP) from a species of the genus Streptomyces. An isolate able to hydrolyze CGP was identified as Streptomyces pratensis strain YSM. The CGPase from S. pratensis strain YSM had an optimum activity at 42 °C and pH 8.5, and was able to degrade CGP at a rate of 12 ± 0.3 µg/mL min. Additionally, this CGPase hydrolyzes water-soluble CGP significantly faster than water-insoluble CGP. The molecular mass of CGPase...
Source
#1Kristine Y. Tan (University of California, Berkeley)
#2Amy E. Herr (University of California, Berkeley)H-Index: 29
In an open microfluidic device, we investigate protein polyacrylamide gel electrophoresis (PAGE) separation performance on single-cell lysate. Single-cell protein electrophoresis is performed in a thin layer of polyacrylamide (PA) gel into which microwells are molded. Individual cells are isolated in these open microwells, then lysed on-chip with a dual lysis and electrophoresis sodium dodecyl sulfate (SDS) buffer. We scrutinize the effect of sieving gel composition on electromigration of protei...
Source
#1Jung Min Kim (KU: Korea University)
#2Baik Lin Seong (Yonsei University)H-Index: 32
Last. Dong-Kwon Lim (KU: Korea University)H-Index: 16
view all 3 authors...
A facile method for the quantification of native state protein is strongly required to accurately determine the amount of expressed protein of interest. Here we report a simple bead-based assay, which can sensitively quantify the amount of native state green fluorescent protein using Ni-NTA (nickel-nitrilotriacetic acid)-modified microbead particles. The bead-based method is simple and straightforward to perform and it showed a highly sensitive capability to detect the expressed fluorescent prot...
Source
#1David Winogradoff (UIUC: University of Illinois at Urbana–Champaign)H-Index: 4
#2Shalini John (UIUC: University of Illinois at Urbana–Champaign)H-Index: 15
Last. Aleksei Aksimentiev (UIUC: University of Illinois at Urbana–Champaign)H-Index: 45
view all 3 authors...
The effects of detergent sodium dodecyl sulfate (SDS) on protein structure and dynamics are fundamental to the most common laboratory technique used to separate proteins and determine their molecular weights: polyacrylamide gel electrophoresis. However, the mechanism by which SDS induces protein unfolding and the microstructure of protein–SDS complexes remain largely unknown. Here, we report a detailed account of SDS-induced unfolding of two proteins—I27 domain of titin and β-amylase—obtained th...
Source
#1Maryam Ghahramani (Shiraz University)H-Index: 3
#2Reza Yousefi (Shiraz University)H-Index: 24
Last. Ali Akbar Moosavi-Movahedi (UT: University of Tehran)H-Index: 41
view all 6 authors...
Abstract In human αB-crystallin (αB-Cry), the highly conserved residues arginine 69 (R69) and aspartate 109 (D109) are located within a critical motif of α-crystallin domain (ACD), contributing to the subunit interactions and oligomeric assembly. Recently, two missense mutations (R69C and D109H) in human αB-Cry have been reported to cause congenital cataract and myopathy disorders. We used various spectroscopic techniques, dynamic light scattering (DLS), small-angle X-ray scattering (SAXS), gel ...
1 CitationsSource
#1Maryam Ghahramani (Shiraz University)H-Index: 3
#2Reza Yousefi (Shiraz University)H-Index: 24
Last. Boris I. Kurganov (RAS: Russian Academy of Sciences)H-Index: 31
view all 4 authors...
Cataract is the major reason for human blindness worldwide. alpha-Crystallin, as a key chaperone of eye lenses, keeps the lenticular tissues in its transparent state over time. In this study, cataract-causing familial mutations, P20R and A171T, were introduced in CRYcapital A, CyrillicB gene. After successful expression in Escherichia coli and subsequent purification, the recombinant proteins were subjected to extensive structural and functional analyses using various spectroscopic techniques, g...
1 CitationsSource