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  • Title: A new purification procedure of human kidney cathepsin H, its properties and kinetic data.
    Author: Popović T, Brzin J, Kos J, Lenarcic B, Machleidt W, Ritonja A, Hanada K, Turk V.
    Journal: Biol Chem Hoppe Seyler; 1988 May; 369 Suppl():175-83. PubMed ID: 3202963.
    Abstract:
    A purification procedure of cathepsin H from human kidney is presented. It includes gel filtration, ion exchange chromatography, and covalent chromatography on thiol Sepharose as an essential step. Purified cathepsin H emerges in an isoelectric focusing gel at pH 6.1 and 6.3. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate shows a molecular mass of about 28 kDa. Less than 20% of the enzyme preparation can be separated into a heavy (24 kDa) and a light chain (4 kDa) after reduction and gel filtration on Sephacryl S-200. The partial amino-acid sequence of human cathepsin H shows its close similarity to rat cathepsin H. Inhibition constants (Ki) of cathepsins H and B with chicken cystatin, two forms of human stefin A, human stefin B, and two forms of human cystatin C are in the range of 10(-9) to 10(-11)M.
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