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A Method for Urinary Trypsin Inhibitor (UTI) Purification Combining Anion-Exchange Chromatography Enrichment and
Gabriele Nieddu1, Marilena Formato1, Antonio Junior Lepedda2
1Department of Biomedical Sciences, University of Sassari, Sassari, Italy.
This chapter describes a method for the purification of urinary trypsin inhibitor (UTI), a small chondroitin sulfate proteoglycan with Ser-proteinase inhibitory activity, excreted at high levels into urine following an inflammatory condition. The method consists of two fractionation steps: an anion-exchange chromatography and a sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) followed by Coomassie Brilliant Blue G-250 gel staining. Several UTI bands are excised from gel, minced, destained, and dehydrated for extraction with SDS-containing buffer, at 60 °C for 24 h. This allows for obtaining a highly purified UTI sample useful for both structural and functional studies.
This chapter describes a method for the purification of urinary trypsin inhibitor (UTI), a small chondroitin sulfate proteoglycan with Ser-proteinase inhibitory activity, excreted at high levels into urine following an inflammatory condition. The method consists of two fractionation steps: an anion-exchange chromatography and a sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) followed by Coomassie Brilliant Blue G-250 gel staining. Several UTI bands are excised from gel, minced, destained, and dehydrated for extraction with SDS-containing buffer, at 60 °C for 24 h. This allows for obtaining a highly purified UTI sample useful for both structural and functional studies.
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