Human spleen cathepsin D: Its characterization and localization in human spleen |
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Institution: | 1. Medical Genetics Branch, National Human Genetics Research Institute, National Institutes of Health, Bethesda, MD, USA |
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Abstract: | - 1.1. The cathepsin D was purified 1830-fold under mild conditions by a rapid procedure, based on two-step affinity chromatography.
- 2.2. Its molecular weight, amino acid composition and substrate specificity were shown to display minor differences from materials of other origins.
- 3.3. Inhibition with thiol compounds was found to be a specific phenomenon of the cathepsin D from the human spleen.
- 4.4. Production of antiserum specific for purified cathepsin D was demonstrated by immunodiffusion test, an immunoadsorbent column and immunoblotting of the crude enzyme in SDS gel.
- 5.5. In an immunocytochemical study, the antigenic sites for this enzyme were found to be localized in the reticuloendothelial system of the human spleen.
- 6.6. The role of this enzyme in human spleen cell was discussed.
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