Richard C, Han K K, Yang H L, Zhu D X, Balduyck M, Mizon J
L'Unité N. 16 de l'INSERM, Faculté de Médicine, Lille, France.
Biomed Chromatogr. 1989 May;3(3):131-5. doi: 10.1002/bmc.1130030309.
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.
