The isolation and the characteristics of serine protease modifier in submandibular gland.

概要

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Serine protease modifier was purified in male mouse submandibular gland using bovine pancreatic trypsin coupled Sepharose 4B affinity chromatography, ion exchange chromatography, gel filtration and chromatofocusing with DfB system. Purified modifier gave the single band in non SDS-polyacrylamide gel electrophrosis and a single peak in HPLC for gel filtration and pI was 9.4, though separated in SDS-polyacrylamide gel electrophrosis into two components, 31KD and 16KD which probably indicate the relationship between monomer and dimer. This molecule has inhibitory coefficient at 0.012 μM to epidermal growth factor binding protein. This inhibitor might act participate in the regulatory system of processing biological active peptide including epidermal growth factor in the mouse submandibular gland.
特定非営利活動法人日本口腔科学会の論文