Isolation and characterization of two new low-molecular-weight protein proteinase inhibitors from the granule-rich fraction of equine neutrophilic granulocytes |
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Authors: | A Pellegrini G H?geli R von Fellenberg |
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Affiliation: | Department of Veterinary Physiology, University of Zürich, Switzerland. |
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Abstract: | A new species of protein proteinase inhibitors was detected in the granule-rich fraction of equine neutrophilic granulocytes. Five isoinhibitors were identified with a narrow enzyme specificity towards two microbial proteinases, e.g., proteinase K and subtilisin. Two isoinhibitors were purified and partially characterized. They had an Mr of 11,300 and 7400, respectively, and were resistant to perchloric acid and heat treatment at 100 degrees C for 20 min. The inhibitors retained their activity over a broad range of pH (1-9 and 1-12, respectively). The possible biological function of this species of protein proteinase inhibitors as defensins (= endogenous antibiotics) is tentatively discussed. |
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