Partial purification and characterisation of sheep mucosal layer proteins

desconocido. The present study was undertaken to partially purify and characterise the sheep mucosal proteins. Cationic proteinswere extracted from mucosal epithelium of sheep intestine, trachea and uterus. Proteins were partially purified by lowpressure liquid chromatography (LPLC) and reverse phase high performance liquid chromatography (RP-HPLC). Theextracts were subjected to 12.5% SDS-PAGE and 15% acid urea polyacrylamide gel electrophoresis for resolving intothe constituent proteins. Different mucosal tissues yielded different concentrations of proteins, lowest from intestineand highest from uterus, which indicated presence of more cationic proteins in sheep uterus than that of sheep intestine.Protein extract of sheep intestine and sheep trachea was separated into 3 peaks each whereas sheep uterus into 4 peaks when subjected to low pressure liquid chromatography. In analytical RP-HPLC, sheep intestinal acid extracted proteins were separated into 6 peaks having elution time of 8.20, 8.41, 8.85, 9.14, 9.52 and 11, and 7 peaks were detected at 6.06, 8.11, 8.42, 8.85, 9.15, 9.47, and 11.30 min in acid extract of sheep tracheal mucosa. When mucosal proteins were subjected to SDS- PAGE 11 protein bands were detected (166.3 kDa to 7.9 kDa) in sheep intestine. 16 bands were detected (166.3 kDa to 9.3 kDa) in sheep uterus and 14 bands were detected (166.3 kDa to 9.3 kDa) in sheep trachea. 166.3 kDa, 117.2 kDa and 100.0 kDa proteins are found common in all the 3 tissues. Acid extract of sheep intestine, sheep uterus and sheep tracheal mucosal layers were separated into 11, 12 and 11 protein bands each respectively, when subjected to 15% acid urea PAGE.