Human Recombinant Pro-dipeptidyl Peptidase I (Cathepsin C) Can Be Activated by Cathepsins L and S but Not by Autocatalytic Processing

Human dipeptidyl peptidase I was expressed in the insect cell/baculovirus system and purified in its active (rhDPPI) and precursor (pro-rhDPPI) forms. RhDPPI was very similar to the purified enzyme (hDPPI) with respect to glycosylation, enzymatic processing, oligomeric structure, CD spectra, and cat...

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Veröffentlicht in:	Biochemistry (Easton) 2001-02, Vol.40 (6), p.1671-1678
Hauptverfasser:	Dahl, Søren W, Halkier, Torben, Lauritzen, Conni, Dolenc, Iztok, Pedersen, John, Turk, Vito, Turk, Boris
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Catalysis Cathepsin B - metabolism Cathepsin C - antagonists & inhibitors Cathepsin C - genetics Cathepsin C - isolation & purification Cathepsin C - metabolism Cathepsin D - metabolism Cathepsin L Cathepsins - metabolism Cattle Chickens Chromatography, Gel Chromatography, High Pressure Liquid Circular Dichroism Cystatin A Cystatin B Cystatin C Cystatins - metabolism Cysteine Endopeptidases Cysteine Proteinase Inhibitors - metabolism Endopeptidases Enzyme Activation - genetics Enzyme Precursors - antagonists & inhibitors Enzyme Precursors - genetics Enzyme Precursors - isolation & purification Enzyme Precursors - metabolism Glycosylation Humans Hydrolysis Molecular Sequence Data Mutagenesis, Site-Directed Protein Processing, Post-Translational Recombinant Proteins - antagonists & inhibitors Recombinant Proteins - biosynthesis Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism
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