タイトル無し
スポンサーリンク
概要
- 論文の詳細を見る
Protease and protease inhibitory activities were estimated in the nasal secretions from chronic sinusitis and nasal allergy, and in the tissue extracts from nasal and paranasal pathological mucosa using 3H-casein as substrate. And their α1. antitripsin and α2-macroglobulin were measured by single radial immunodiffusion assay.Considerably high protease activities were revealed in the secretions from chronic sinusitis, low in the tissue extracts and less in the secretions of nasal allergy. It was presumed that the greater part of proteases of nasal purulent secretions seemed to be originated from granulocyte elastase because of their optimal pH and reactions against ethylenediaminetetraacetic acid (EDTA), L-cystein, phenylmethylsulfonyl fluoride (PMSF) and ovomucoid trypsin inhibitor.The α1-antitrypsin and α2-macroglobulin determined in the secretions from chronic Sinusitis and in tissue extracts were not detected in the secretions of nasal allergy, in which trypsin inhibitory activities were remarkably higher. Furthermore, a low molecular weight protease inhibitor was partially isolated from the secretions of nasal allergy by gel chromatography and characterized. This protease inhibitor which had an apparent molecular weight of 10, 000 daltons in sodium dodecyl sulfate gel electrophoresis showed inhibitory activities against bovine pancreatic trypsin and chymotrypsin, and proteases from the purulent secretions of the nose, but not against porcine pancreatic clastase, human plasmin and papain. These results could be suggested that a low molecular weight protease inhibitor from allergic nasal secretions might be related to that of granulocytes, especially to eosinophils.
- 一般社団法人 日本耳鼻咽喉科学会の論文