Synthesis, cloning and expression in Escherichia coli of the gene coding for the trypsin inhibitor from Cucurbita pepo.
A chemically synthesized gene coding for the serine proteinase inhibitor CPTI II was cloned in E. coli and its expression was investigated in cytoplasmic and secretion systems. Under all conditions investigated the biologically active form of the inhibitor was found only in the latter system, although the yield was rather low.
Rempoøa
B
B
Institute of Biochemistry and Biophysics of the Polish Academy of Sciences, Warsaw.
Wilusz
T
T
Markiewicz
W
W
Fikus
M
M
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics; D001483:Base Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D005813:Genes, Synthetic; D005822:Genetic Vectors; D007544:Isopropyl Thiogalactoside / Q000494:pharmacology; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000096:biosynthesis* / Q000235:genetics; D021382:Protein Sorting Signals; D015183:Restriction Mapping; D015842:Serine Proteinase Inhibitors / Q000096:biosynthesis* / Q000235:genetics; D013696:Temperature; D013997:Time Factors; D014357:Trypsin / Q000378:metabolism; D014361:Trypsin Inhibitors / Q000096:biosynthesis* / Q000235:genetics; D014675:Vegetables / Q000235:genetics*
D001425:Bacterial Outer Membrane Proteins; C048467:CPTI-II protein, Cucurbita pepo; D010940:Plant Proteins; D021382:Protein Sorting Signals; D015842:Serine Proteinase Inhibitors; D014361:Trypsin Inhibitors; D007544:Isopropyl Thiogalactoside; D014357:Trypsin