Characterization of peptic inhibitory activity associated with sulfated glycoprotein isolated from gastric mucosa
作者： Yuko Mikuni-Takagaki , Kyoko Hotta
DOI: 10.1016/0304-4165(79)90274-5
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摘要: Abstract Sulfated glycoproteins were extracted and purified from porcine stomach mucous scraping. Four sulfated glycoprotein fractions separated subsequently purified. These compounds always accompanied the apparent peptic inhibitory activity consisted of 15–18% (w/w) protein. The carbohydrate portions contained an equimolar ratio galactose hexosamine (mainly glucosamine), together with lesser amounts fucose sialic acid. sulfate content above was 2–9% total glycoprotein. mode inhibition to investigated suggested that there binding substrate pepsin, making resistant activity. neither bound pepsin at pH 1.8 nor inhibited hydrolysis a synthetic dipeptide pepsin. Desulfation resulted in loss both precipitate formation. precipitation curve for serum albumin showed varying proportions suggests components are multivalent this
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