An epidemiological study of diagnostic and therapeutic strategies in office practice patients with subacute or chronic pain in the thoracic or low back. Comparison of practices in primary care and rheumatology settings

Mucin was purified by the gel filtration method on columns with high porous molecular sives in buffers with SDS and proteinase inhibitors. The addition of proteinase inhibitors distinctly inhibited proteolytic activity. It was found that the obtained mucin, after disulphide-bound reduction, is dissociated to mucin subunits and N-glycosylated glycoprotein of molecular weight about 75 kDa. This protein has carbohydrate and amino acid composition different from high molecular fraction. The 75 kDa protein is strongly associated with high molecular mass mucin subunits and can be separated either during electrophoresis or fractionation in buffers with 2-mercaptoethanol.