Extractability of lysozyme from bovine nasal cartilage
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چکیده
منابع مشابه
Characteristics of the nonaggregating proteoglycans isolated from bovine nasal cartilage.
Purified proteoglycans from bovine nasal cartilage (the Al fraction) were separated by sedimentation velocity centrifugation into a fraction enriched in aggregates (Al-Sl) and a fraction of nonaggregated proteoglycans (Al-S2), containing about 85% and 15% of the starting material, respectively. Both fractions were centrifuged in a dissociative CsCl density gradient to remove non-proteoglycan pr...
متن کاملPhysical properties and polydispersity of proteoglycan from bovine nasal cartilage.
Eighty per cent of the proteoglycan of bovine nasal cartilage can be recovered in a purified preparation known as proteoglycan subunit; the preparation contains 87% chondroitin sulfate, 6% keratan sulfate, and 7% protein. The physical properties of proteoglycan subunit are not affected by exposure to 4 M guanidinium chloride, to reducing agents, or to pH 2.7. Proteoglycan subunit contains a sin...
متن کاملThe isolation of collagen-associated molecules from bovine nasal cartilage.
Chung, E. & Miller, E. J. (1974) Science 183,1200-1201 Dehm, P. & Prockop, D. J. (1971) Biochim. Biophys. Acta 240,358-369 Dehm, P. & Prockop, D. J. (1972) Biochim. Biophys. Acta 264,375-382 Dehm, P. & Prockop, D. J. (1973) Eur. J. Biochem. 35,159-166 Grant, M. E., Kefalides, N. A. & Prockop, D. J. (1972) J. Biol. Chem. 247,3545-3551 Grant, M. E., Harwood, R. & Schofield, J. D (1974) in Dynamic...
متن کاملThe Fine Structure of Bovine Nasal Cartilage
Bovine nasal cartilage was studied by electron microscopy before and after extraction with 4 M guanidinium chloride or 1.9 M CaCl(2). These solvents removed matrix granules, basophilia, and 85% of the proteoglycan complex, measured as hexuronate. Simultaneously, many collagen fibrils were disaggregated into component microfibrils (approximately 40 A thick). In contrast to the above solvents, ex...
متن کاملProteinase inhibitors of bovine nasal cartilage.
Extracts from bovine nasal cartilage with 1 M-guanidinium chloride were fractionated by ultrafiltration. Gel chromatography of the low-molecular-weight material resolved three distinct fractions with inhibitory activity against (a) collagenases (22000 mol.wt.), (b) thiol proteinases cathepsin B and papain (13000 mol.wt.), and (c) trypsin and other serine proteinases (7000 mol.wt.).
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Enzymology
سال: 1972
ISSN: 0005-2744
DOI: 10.1016/0005-2744(72)90141-6