Canduri F, Ward R J, de Azevedo Júnior W F, Gomes R A, Arni R K
Departamento de Física, IBILCE/UNESP, São José do Rio Preto, Brazil.
Biochem Mol Biol Int. 1998 Jul;45(4):797-803. doi: 10.1080/15216549800203222.
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 Kcat of 14.3 s-1 and a kcat/KM of 2.70 x 10(6) s-1M-1 as determined by the hydrolysis of a fluorogenic peptide substrate.
