Isolation and Partial Characterization of a Low Molecular Weight Acid Stable Protease Inhibitor from Human Bronchial Secretion

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Abstract
An acid stable protease inhibitor was isolated from human bronchial secretion. Two important stages of the purification procedure were affinity chromatography on trypsin bound to Affi-Gel 10 and ion-exchange chromatography on SP-Sephadex C-50. The isolated inhibitor appeared as a single band on analytical disc electrophoresis and eluted as a homogeneous protein peak on gel filtration on Sephadex G-75 corresponding to a MW of about 10,500. Amino acid analyses showed no tryptophan or histidine and as N-terminal amino acid tyrosine. No glucosamine or galactosamine was detected. The results of the analyses suggest that the purified inhibitor is identical to the low MW trypsin-chymotrypsin inhibitor of human seminal plasma (HUSI-I).

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