Spinach chloroplast ATP-dependent endopeptidase: Ti-like protease.
The soluble fraction of spinach chloroplast was used for purification and characterization of an ATP-dependent protease. Purification included Q Sepharose Fast Flow, hydroxylapatite and FPLC Superose 6 column chromatography. The isolated enzyme requires ATP and Mg2+ for stimulation and represents a ubiquitin independent serine protease, containing essential sulphydryl group(s). By using fluorogenic peptides a similarity of chloroplast protease to Escherichia coli Ti protease was observed. The chloroplast protease is immunochemically cross-reactive with the bacterial protease Ti.
Benesová
M
M
Department of Cell and Molecular Biology of Drugs, Faculty of Pharmacy, Comenius University, Bratislava, Slovak Republic.
Durcová
G
G
Kuzela
S
S
Kutejová
E
E
Psenák
M
M
D049069:ATP-Dependent Proteases; D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D002736:Chloroplasts / Q000201:enzymology*; D002845:Chromatography; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003429:Cross Reactions; D017886:Durapatite; D004926:Escherichia coli / Q000201:enzymology; D006360:Heat-Shock Proteins / Q000302:isolation & purification* / Q000378:metabolism*; D007700:Kinetics; D008274:Magnesium / Q000378:metabolism; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000378:metabolism; D012697:Serine Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism*; D018724:Spinacia oleracea / Q000201:enzymology*; D013379:Substrate Specificity
D006360:Heat-Shock Proteins; D009842:Oligopeptides; D000255:Adenosine Triphosphate; D017886:Durapatite; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases; D008274:Magnesium