sodium-dodecyl-sulfate and succinic-anhydride

sodium-dodecyl-sulfate has been researched along with succinic-anhydride* in 1 studies

Other Studies

1 other study(ies) available for sodium-dodecyl-sulfate and succinic-anhydride

Article	Year
Evidence for the overestimation of molecular masses of proteins after chemical modification and chemical crosslinks on sodium dodecyl sulfate/polyacrylamide gel electrophoresis (SDS-PAGE). Biomedical chromatography : BMC, 1989, Volume: 3, Issue:3 Human trypsin inhibitor (home prepared), lactalbumin, trypsinogen, carbonic anhydrase, and bovine serum albumin were submitted to succinylation and their molecular masses were determined by SDS-PAGE according to the method of Weber and Osborn (1969 J. Biol. Chem. 244, 4406) before and after chemical modification. High estimates of their molecular masses were obtained. The monomer and dimer of arrowhead inhibitor proteinase-B (Chinese vegetable legume) obtained after chemical crosslink(s) were also submitted to SDS-PAGE and their apparent molecular masses were also determined and compared to the native arrowhead inhibitor proteinase-B. Abnormally high estimates of their molecular masses were obtained. Our results agree with those in the literature. Topics: Carbon Radioisotopes; Cross-Linking Reagents; Electrophoresis, Polyacrylamide Gel; Indicators and Reagents; Molecular Weight; Proteins; Sodium Dodecyl Sulfate; Succinic Anhydrides	1989

Article

Year

Evidence for the overestimation of molecular masses of proteins after chemical modification and chemical crosslinks on sodium dodecyl sulfate/polyacrylamide gel electrophoresis (SDS-PAGE).

Biomedical chromatography : BMC, 1989, Volume: 3, Issue:3

Human trypsin inhibitor (home prepared), lactalbumin, trypsinogen, carbonic anhydrase, and bovine serum albumin were submitted to succinylation and their molecular masses were determined by SDS-PAGE according to the method of Weber and Osborn (1969 J. Biol. Chem. 244, 4406) before and after chemical modification. High estimates of their molecular masses were obtained. The monomer and dimer of arrowhead inhibitor proteinase-B (Chinese vegetable legume) obtained after chemical crosslink(s) were also submitted to SDS-PAGE and their apparent molecular masses were also determined and compared to the native arrowhead inhibitor proteinase-B. Abnormally high estimates of their molecular masses were obtained. Our results agree with those in the literature.

Topics: Carbon Radioisotopes; Cross-Linking Reagents; Electrophoresis, Polyacrylamide Gel; Indicators and Reagents; Molecular Weight; Proteins; Sodium Dodecyl Sulfate; Succinic Anhydrides

1989