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Evidence for the overestimation of molecular masses of proteins after chemical modification and chemical crosslinks on sodium dodecyl sulfate/polyacrylamide gel electrophoresis (SDS‐PAGE)
Author(s) -
Richard Claude,
Han KiaKi,
Yang HuiLing,
Zhu DeXu,
Balduyck Malika,
Mizon Jacques
Publication year - 1989
Publication title -
biomedical chromatography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.4
H-Index - 65
eISSN - 1099-0801
pISSN - 0269-3879
DOI - 10.1002/bmc.1130030309
Subject(s) - chemistry , sodium dodecyl sulfate , succinylation , molecular mass , chromatography , trypsin inhibitor , polyacrylamide gel electrophoresis , monomer , chemical modification , gel electrophoresis , dimer , trypsin , biochemistry , organic chemistry , enzyme , amino acid , polymer , lysine
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.