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Glycosylation of procathepsin L does not account for species molecular-mass differences and is not required for proteolytic activity
S. M. Smith
, S. E. Kane
, S. Gal
, R. W. Mason
, M. M. Gottesman
Penn State Harrisburg
Research output
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Contribution to journal
›
Article
›
peer-review
26
Scopus citations
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Dive into the research topics of 'Glycosylation of procathepsin L does not account for species molecular-mass differences and is not required for proteolytic activity'. Together they form a unique fingerprint.
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Keyphrases
Proteolytic Activity
100%
Molecular Mass
100%
Glycosylation
100%
Mass Difference
100%
Two-species
40%
Cathepsin L
40%
Endoglycosidase H
40%
High Concentration
20%
NIH3T3
20%
Complementary DNA (cDNA)
20%
Transfectant
20%
Mouse Cells
20%
Human Cells
20%
SDS-polyacrylamide Gel
20%
Cysteine Protease
20%
Enzymatic Activity
20%
Pulse-chase
20%
Inhuman
20%
Neuroscience
Glycosylation
100%
Cathepsin L
40%
Transfection
20%
In Vitro
20%
Enzyme Activity
20%
Polyacrylamide
20%
Cysteine Protease
20%
Enzyme Precursor
20%
Glycosylated Protein
20%