A Rapid Two-Step Purification of Rat Cystatin C,One Major Inhibitor of Cysteine Proteinases |
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| Authors: | Catherine Tavera Jean-Claude Guillemot Joël Capdevielle Pascual Ferrara Jeanne Leung-Tack Allain Collé |
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| Affiliation: | 1. Atatürk üniversty Science, Art Faculty Chemistry Department , 25240, Erzurum, Turkiye;2. Atatürk üniversty, Medical Faculty Biochemistry Department , 25240, Erzurum, Turkiye |
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| Abstract: | ABSTRACT Rat cystatin C was purified to apparent homogeneity from rat urine after induction of a tubular dysfunction with sodium chromate. Twentyfold concentrated urine was chromatographed by a rapid purification procedure. A two-step purification including affinity chromatography on carboxymethyl papain- Sepharose and high-resolution anion exchange chromatography was developped. The purified protein has an apparent molecular mass of 15 kDa and pI of 10.2; its aminoacid composition was similar to human cystatin C. As opposed to previous data, purified urinary rat cystatin C did not contain significant amounts of carbohydrate. Antisera against rat cystatin C, raised in rabbits, partially cross-reacted with human and mouse cystatin C, indicating their antigenic similarities. Like human cystatin C, native rat cystatin C, named slow form, is degraded into a more acidic form, called fast form, by a loss of N-terminal amino acids; fast form displayed a pI of 9.4. |
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