Document Detail

Molecular forms of cathepsin D in coated vesicle preparations.
MedLine Citation:
PMID:  6138304     Owner:  NLM     Status:  MEDLINE    
We have studied the polypeptide pattern of cathepsin D associated with coated vesicle fractions prepared from human placenta. In these fractions cathepsin D was about 35-fold enriched in the precursor polypeptides as compared to the unfractionated tissue extract. The enrichment was more prominent if the vesicles were fractionated in the presence of Triton X-100. Adsorption of exogenously added metabolically labelled cathepsin D precursor to the fractionated material was negligible. It is likely that the precursor and may be also the mature cathepsin D polypeptides are present in the matrix of the coated vesicles. This finding substantiates the idea that coated vesicles participate in the transport of newly synthesized cathepsin D into the lysosomes.
S Tümmers; M Zühlsdorf; H Robenek; A Hasilik; K von Figura
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Hoppe-Seyler's Zeitschrift für physiologische Chemie     Volume:  364     ISSN:  0018-4888     ISO Abbreviation:  Hoppe-Seyler's Z. Physiol. Chem.     Publication Date:  1983 Sep 
Date Detail:
Created Date:  1983-12-20     Completed Date:  1983-12-20     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985060R     Medline TA:  Hoppe Seylers Z Physiol Chem     Country:  GERMANY, WEST    
Other Details:
Languages:  eng     Pagination:  1287-95     Citation Subset:  IM    
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MeSH Terms
Cathepsin D
Cathepsins / isolation & purification,  metabolism*
Cell Fractionation
Centrifugation, Density Gradient
Coated Pits, Cell-Membrane / enzymology*,  ultrastructure
Endosomes / enzymology*
Lysosomes / enzymology
Microscopy, Electron
Placenta / enzymology*
Reg. No./Substance:
EC 3.4.-/Cathepsins; EC D

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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