Partial purification and characterization of the tissue plasminogen activator in nasal mucosa and nasal polyp.

Tissue plasminogen activator was partially purified from the inferior turbinate and nasal polyp, and its biochemical properties were investigated. Similar TPA peak positions were seen in the gel filtration chromatography of both tissues, and the molecular weight was approximately 65,000, which was comparable to TPA of pig heart (55,000-60,000). Activity of TPA from inferior turbinate was higher than that from nasal polyp. TPA from both tissues was completely inhibited by trans-aminomethyl cyclohexane carboxylic acid, dithiothreitol, and diisopropylfluorophosphate and had similar inhibition profiles to TPA from pig heart. All these findings indicate that TPA from both tissues is undoubtedly a plasminogen-activating enzyme and serine-type protease and would be biochemically identical.