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Amino‐terminal heterogeneity of E. coli TEM‐β‐lactamase secreted from Bacillus subtilis
Author(s) -
Kalkkinen Nisse,
Sibakov Mervi,
Sarvas Matti,
Palva Ilkka,
Kääriäinen Leevi
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80502-6
Subject(s) - bacillus subtilis , plasmid , recombinant dna , transformation (genetics) , cleavage (geology) , dna , escherichia coli , bacillaceae , sequence (biology) , hybrid plasmid , signal peptide , biology , bacillales , peptide sequence , chemistry , biochemistry , bacteria , genetics , gene , paleontology , fracture (geology)
E.coli TEM‐β‐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.