Amino-terminal heterogeneity of E. coli TEM-beta-lactamase secreted from Bacillus subtilis.
E. coli TEM-beta-lactamase, secreted from Bacillus subtilis after transformation with three different hybrid plasmids, was purified and subjected to direct amino-terminal sequence analysis. The results show that the signal sequence cleavage site varies depending on the hybrid plasmid construction and cannot be exactly predicted from the DNA sequences. The results are of general interest if recombinant DNA technology is used to synthesize, e.g. pharmaceutical products where the preservation of the authentic amino-terminal structure is highly desirable.
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D005822:Genetic Vectors; D014169:Transformation, Bacterial; D001618:beta-Lactamases / Q000235:genetics* / Q000302:isolation & purification
D001618:beta-Lactamases