Over-production and isolation of a precursor protein in a form ideal as a substrate for leader peptidase.
Kaderbhai
N N
NN
Institute of Biological Sciences, University of Wales, Aberystwyth, Dyfed.
Harding
V J
VJ
Kaderbhai
M A
MA
D000469:Alkaline Phosphatase / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D003001:Cloning, Molecular; D015786:Cytochromes b5 / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*; D010450:Endopeptidases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology; D008099:Liver / Q000378:metabolism; D008565:Membrane Proteins; D011498:Protein Precursors / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*; D021382:Protein Sorting Signals / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism; D012697:Serine Endopeptidases; D013379:Substrate Specificity
D008565:Membrane Proteins; D011498:Protein Precursors; D021382:Protein Sorting Signals; D011993:Recombinant Fusion Proteins; D015786:Cytochromes b5; D000469:Alkaline Phosphatase; D010450:Endopeptidases; D012697:Serine Endopeptidases; C026515:type I signal peptidase