Proteins and Sodium Dodecyl Sulfate: Molecular Weight Determination on Polyacrylamide Gels and Related Procedures

Weber, K; Osborn, Mary

doi:10.1016/b978-0-12-516301-9.50007-3

Cited by 423 publications

(230 citation statements)

References 68 publications

Supporting

Mentioning

220

Contrasting

Unclassified

Order By: Relevance

“…labeled with l 2 P I (New England Nuclear, Boston, MA), by SDS-PAGE. Using cylindrical gels, SDS-PAGE was performed according to the method of Weber and Osborne (22). with an acrylamide concentration of 5%.…”

Section: Methodsmentioning

confidence: 99%

The immunoreactivity, ligand, and cell binding characteristics of rheumatoid synovial fluid fibronectin

Carsons

Lavietes

Diamond

et al. 1985

Arthritis & Rheumatism

View full text Add to dashboard Cite

Fibronectin promotes macrophage adherence and expression of Fc receptors, is chemotactic for fibroblasts, and is an opsonin for fibrin and denatured collagen. These properties suggest a role for fibronectin in the modulation of joint inflammation. Since structural modification of the fibronectin molecule has been shown to result in loss or de novo acquisition of opsonic and chemotactic activity, we determined the functional and immunochemical properties of fibronectin isolated from the inflamed joint. Eighty‐six percent of synovial fluids obtained from patients with active rheumatoid arthritis (RA) contained fibronectin fragments, and 39% of the fluids no longer displayed the dimeric form. Compared with native fibronectin, RA peptides were as active in promoting synoviocyte chemotaxis and in glycosaminoglycan binding, but displayed lower affinity for fibrin and gelatin. Although comparable with intact protein in augmenting monocyte attachment to gelatin, the RA synovial fluid peptides did not augment monocyte attachment to fibrin. Analysis of whole synovial fluid and isolated fibronectins by enzyme immunoassay showed that the increased fibronectin immunoreactivity, previously reported in RA synovial fluid, measures intact and nearly intact protein and does not measure extensively degraded fragments.

show abstract

Section: Methodsmentioning

confidence: 99%

The immunoreactivity, ligand, and cell binding characteristics of rheumatoid synovial fluid fibronectin

Carsons

Lavietes

Diamond

et al. 1985

Arthritis & Rheumatism

View full text Add to dashboard Cite

show abstract

“…These observations suggest that citrullination of arginine residues decreases the positive charge, follows conformational change, and leads to a mobility shift on SDS-PAGE [13][14][15].…”

Section: Sds-page Conditions But Citrullinated Fibrinogen Did Not Unmentioning

confidence: 99%

Citrullinated fibrinogen shows defects in FPA and FPB release and fibrin polymerization catalyzed by thrombin

Okumura¹,

Haneishi²,

Terasawa³

2009

Clinica Chimica Acta

View full text Add to dashboard Cite

“…The SDS-Tris/glycine pH 8-3 system (Laemmli, 1970) was used and protein bands were stained with Coomassie Brilliant Blue R250, as described by Weber & Osborn (1975). Final acrylamide concentrations (w/v) of 10% (for whole cells and membranes) or 15% (for soluble fractions) were used.…”

Section: Sds-pagementioning

confidence: 99%

Characterization of a novel soluble c-type cytochrome in a moxD mutant of Methylobacterium extorquens AM1

Day

Nunn²,

Anthony³

1990

Journal of General Microbiology

View full text Add to dashboard Cite

Methylobacterium extorquens AM1 contains a novel c-type cytochrome, called cytochrome c-553, previously thought to be a precursor of the electron acceptor (cytochrome cL) for methanol dehydrogenase. Its amino acid composition and serological characteristics show that it has no structural relationship to cytochrome cL. It usually comprises less than 5% of the total c-type cytochromes. In a moxD mutant, which contains neither methanol dehydrogenase nor cytochrome cL, it comprises 30% of the soluble cytochrome and it has been purified and characterized from that mutant. Cytochrome c-553 is large ( M , 23000), acidic and monohaem, with a redox potential of 194 mV. It reacts rapidly and completely with CO but is not autoxidizable. It is not autoreducible, and it is not an electron acceptor from methanol dehydrogenase or methylamhe dehydrogenase, nor an important electron donor to the oxidase. It is able to accept electrons from cytochrome cL and to donate electrons to cytochrome cH. It is present in the soluble fraction (presumably periplasmic) and membrane fraction of wild-type bacteria during growth on a wide range of growth substrates, but its function in these bacteria or in the moxD mutant has not been determined.

show abstract

Proteins and Sodium Dodecyl Sulfate: Molecular Weight Determination on Polyacrylamide Gels and Related Procedures

Cited by 423 publications

References 68 publications

The immunoreactivity, ligand, and cell binding characteristics of rheumatoid synovial fluid fibronectin

The immunoreactivity, ligand, and cell binding characteristics of rheumatoid synovial fluid fibronectin

Citrullinated fibrinogen shows defects in FPA and FPB release and fibrin polymerization catalyzed by thrombin

Characterization of a novel soluble c-type cytochrome in a moxD mutant of Methylobacterium extorquens AM1

Contact Info

Product

Resources

About