Purification and characterization of a serine proteinase inhibitor from human articular cartilage |
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| Institution: | 1. Laboratory of Aquatic Environmental Research, Centro de Estudios Avanzados, Universidad de Playa Ancha, Viña del Mar, Chile;2. HUB-AMBIENTAL UPLA, Universidad de Playa Ancha, Valparaíso, Chile;3. Doctorado Interdisciplinario en Ciencias Ambientales, Facultad de Ciencias Naturales y Exactas, Universidad de Playa Ancha, Valparaíso, Chile;4. Doctorado en Ciencias del Mar y Biología Aplicada, Departamento de Ciencias del Mar y Biología Aplicada, Universidad de Alicante, Alicante, Spain;5. Centro de Recursos Hídricos para la Agricultura y Minería, Universidad de Concepción, Concepción, Chile;6. Doctorado en Ciencias Ambientales, Centro EULA, Universidad de Concepción, Concepción, Chile;7. Centro de Bioinnovación, Universidad de Antofagasta, Antofagasta, Chile;8. Laboratorio de Toxicología Acuática (AQUATOX), Instituto de Ciencias Naturales Alexander von Humboldt, Universidad de Antofagasta, Antofagasta, Chile;9. Departamento de Ingeniería Química, Universidad de Alicante, Alicante, Spain;10. Departamento de Ciencias del Mar y Biología Aplicada, Universidad de Alicante, Alicante, Spain;1. Cardiovascular Performance Program, Massachusetts General Hospital, Boston, Mass;2. Harvard T.H. Chan School of Public Health, Boston, Mass;3. Channing Division of Network Medicine, Brigham and Women''s Hospital, Boston, Mass;4. Emory Clinical Cardiovascular Research Institute, Emory University School of Medicine, Atlanta, Ga;5. Department of Medical Oncology, Dana-Farber Cancer Institute, Boston, Mass;6. Department of Neurology, Beth Israel Deaconess Medical Center, Boston, Mass;7. Department of Physical Medicine and Rehabilitation, Spaulding Rehabilitation Hospital, Boston, Mass |
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| Abstract: | An inhibitor of serine proteinases from human articular cartilage was purified to homogeneity by sequential ultrafiltration and ion exchange chromatography on CM-Sephadex C-50. The apparent molecular weight of the cationic glycoprotein (pI > 10) was determined to be 16.5 · 103 by SDS gel electrohoresis. The inhibitor blocked the activity of leukocyte elastase, cathepsin G and trypsin but not leukocyte collagenase. In kinetic studies for the interactions with leukocyte elastase a firm enzyme-inhibitor binding was obtained. Amino acid analyses did not reveal homologies with other serine proteinase inhibitors already purified from human tissues. |
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