Abstract
Upon detergent or hypo-osmotic lysis of CHO-cell postnuclear supernatants or isolated lysosomes at pH 4.8, the lysosomal enzymes beta-hexosaminidase, beta-galactosidase, alpha-fucosidase and cathepsin C were readily pelleted, whereas the exogenous marker, long-term-internalized horseradish peroxidase, was not. Salt or pH elevation greatly decreased lysosomal-enzyme pelletability. The results suggest that, under native conditions, lysosomal hydrolases may be aggregated. Aggregation could promote enzyme retention within the organelle.
MeSH Terms
Animals
Cathepsin C
Cell Line
Centrifugation, Density Gradient
Cricetinae
Cricetulus
Detergents/pharmacology
Dipeptidyl-Peptidases and Tripeptidyl-Peptidases/metabolism
Galactosidases/metabolism
Hydrogen-Ion Concentration
Lysosomes/drug effects,enzymology
Macromolecular Substances
Sodium Chloride/pharmacology
alpha-L-Fucosidase/metabolism
beta-Galactosidase/metabolism
beta-N-Acetylhexosaminidases/metabolism
Chemicals
Detergents
Macromolecular Substances
Sodium Chloride
Galactosidases
beta-Galactosidase
alpha-L-Fucosidase
beta-N-Acetylhexosaminidases
Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
Cathepsin C
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Buckmaster M J
Department of Biochemistry and Nutrition, Virginia Polytechnic Institute and State University, Blacksburg 24061.
Ferris A L
Storrie B
References (15)
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