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Human placental cathepsin D has been purified 6000-fold and its properties characterized. Its molecular weight has been ascertained to be 42 000 by gel filtration and 43 300 by analytical ultracentrifugation. SDS gel electrophoresis in the presence of beta-mercaptoethanol cleaves the enzyme into two polypeptides of molecular weights 28 200 and 14 400. The placental enzyme resembles cathepsin D isolated from other mammalian tissues in many of its properties, including pH optimum. The higher degree of purification has led to a shift in the isoelectric points of the three isoenzymes from those recorded by other authors. Antibodies raised against cathepsin D in rabbits inhibit it at pH 5.0, and the inhibition is almost 100 per cent with adequate concentrations of monospecific antibody.
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R M Mason, and
M Oakey
March 1974,
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January 1963,
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S F Contractor, and
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July 1992,
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April 1979,
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August 1976,
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September 1995,
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology,
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M Oakey
August 1988,
Biological chemistry Hoppe-Seyler,
S F Contractor, and
R M Mason, and
M Oakey
February 1974,
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S F Contractor, and
R M Mason, and
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November 1983,
Biochemistry,
