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pubmed-article:8876448pubmed:abstractTextA rapid and simple method for analyzing cathepsin D in breast tissue based on capillary zone electrophoresis (CZE) is described. After incubating the tissue extracts with hemoglobin as a substrate, a specific peptide is cleaved and separated by CZE in less than 5 min. This peptide is not produced by the action of pepsin or trypsin. It is inhibited by the addition of pepstatin, a specific inhibitor for cathepsin D. Human hemoglobin acted as a better substrate than bovine hemoglobin. The test compared well to a radioimmunoassay. We have shown that peptides can be stacked by the use of acetonitrile. The method demonstrates the advantages of CZE for assay of proteolytic enzymes in general.lld:pubmed
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pubmed-article:8876448pubmed:authorpubmed-author:ShihabiZ KZKlld:pubmed
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pubmed-article:8876448pubmed:dateRevised2007-10-16lld:pubmed
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pubmed-article:8876448pubmed:articleTitleAnalysis of cathepsin D from breast tissues by capillary electrophoresis.lld:pubmed
pubmed-article:8876448pubmed:affiliationDepartment of Pathology, Bowman Gray School of Medicine, Wake Forest University, Winston-Salem, NC 27157, USA.lld:pubmed
pubmed-article:8876448pubmed:publicationTypeJournal Articlelld:pubmed