Protein content of molar–incisor hypomineralisation enamel

Objectives m of the study was to compare the relative amounts and nature of the proteinous content of sound and molar–incisor hypomineralisation (MIH) enamel. s 0%) was used to dissolve the mineral phase and precipitate the proteins from enamel pieces sectioned from sound and MIH enamel. The protein content was estimated using a miniaturized version of the method of Lowry et al. Samples of the solubilised protein were separated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), stained with Coomassie Blue R250 and tryptic fingerprint/mass spectrometry (MS/MS) of bands in excised gel pieces used for protein identification. s ed to sound enamel, brown enamel showed a 15–21-fold higher protein content, and yellow and chalky enamel showed about 8-fold higher protein content. Tryptic fingerprint/MS performed on excised 50–70 kDa areas demonstrated serum albumin, type I collagen and antitrypsin to be common to all types of enamel. Yellow and brown enamel showed more abundant serum albumin and antitrypsin, and the presence of serum antithrombin. Albumin is reported to be an inhibitor of crystal growth, and antitrypsin and antithrombin inhibit kallikrein 4 proteolytic activity. sions mbination of the effects of serum proteins on developing enamel may result in elevated proteinous content and reduced mineral content as seen in MIH enamel.