Purification and partial characterization of cathepsin D from porcine (Sus scrofa) liver using affinity chromatography
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Undergraduate course
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Academic Press Aust
Wiley
Wiley
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Article
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Acesso aberto
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Abstract
Cathepsin D, a lysosomal aspartic protease, has been purified from porcine liver using a combination of pepstatin-A agarose and Affi-Gel Blue affinity chromatography, followed by size-exclusion chromatography. The purified protein consists of two polypeptide chains of 15 and 30 kDa, and has an isoelectric point of 6.8. Porcine liver cathepsin D has maximum activity at pH 2.5-3.0 as determined by its activity against hemoglobin, with a K-cat of 14.3 s(-1) and a k(cat)/K-M of 2.70 x 10(6) s(-1) M-1 as determined by the hydrolysis of a fluorogenic peptide substrate.
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English
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Biochemistry and Molecular Biology International. Marrickville: Academic Press Aust, v. 45, n. 4, p. 797-803, 1998.
