Human placental cathepsin B1. Isolation and some physical properties |
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| Authors: | Arnold A. Swanson Bill J. Martin Sam S. Spicer |
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| Affiliation: | Departments of Biochemistry, Ophthalmology and Pathology, The Medical University of South Carolina, Charleston, S.C. 29401, U.S.A. |
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| Abstract: | A reproducible procedure for the isolation, from human placenta, of a cathepsin B1 in a homogeneous state, demonstrated by electrophoretic, ultracentrifugal and enzymic criteria, was carried out. The pH optimum was near pH5.5. The placental enzyme catalysed the release of acid-soluble u.v.-dense products from haemoglobin and myoglobin. It was inhibited by heavy metals and several compounds which react with the thiol groups. The optimum temperature was between 37° and 42°C. The molecular weight of the enzyme was calculated to be 24250. |
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