The inhibition of cytochrome oxidase by lysosomal cationic proteins of rabbit polymorphonuclear leukocytes |
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| Authors: | R Penniall J P Holbrook H I Zeya |
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| Affiliation: | 1. Department of Biochemistry, University of North Carolina, Chapel Hill, N.C. 27514 USA;2. Department of Bacteriology, University of North Carolina, Chapel Hill, N.C. 27514 USA;1. School of Chemistry and Chemical Engineering and Institute of Biotechnology, Shanxi University, Taiyuan 030006, China;2. State Key Laboratory of Solid Waste Reuse for Building Materials, Beijing 100041, China;1. Shanxi Key Laboratory of Otorhinolaryngology Head and Neck Cancer, First Hospital of Shanxi Medical University, Taiyuan 030001, Shanxi, PR China;2. Shanxi Province Clinical Medical Research Center for Precision Medicine of Head and Neck Cancer, First Hospital of Shanxi Medical University, Taiyuan 030001, Shanxi, PR China;3. Department of Otolaryngology Head & Neck Surgery, First Hospital of Shanxi Medical University, Taiyuan 030001, Shanxi, PR China;4. Department of Cell biology and Genetics, the Basic Medical School of Shanxi Medical University, Taiyuan 030001, Shanxi, PR China;5. Department of Anatomy, the Basic Medical School of Shanxi Medical University, Taiyuan 030001, Shanxi, PR China |
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| Abstract: | At 0.33 μM, a mixture of cationic proteins from PMN lysosomes decreased the velocity constant of rat liver cytochrome oxidase by 50%. Separation of the proteins into fractions of circa 8000 and 4000 M.W. reveals that the former is the more potent in its inhibition of cytochrome oxidase, causing 50% inhibition of activity at 0.1 μM. |
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