TY - JOUR
T1 - The study of biogenesis and secretion of alkaline phosphatase and its mutant forms in Escherichia coli. I. Introduction of mutations into alkaline phosphatase gene
AU - Karamyshev, A. L.
AU - Shlyapnikov, M. G.
AU - Khmelnitsky, M. I.
AU - Nesmeyanova, M. A.
AU - Ksenzenko, V. N.
PY - 1994
Y1 - 1994
N2 - Various mutations in E. coli alkaline phosphatase gene were obtained by oligonucleotide-directed mutagenesis. They result in amino acid substitutions in the signal peptide cleavage site [Val for Ala(-1)] and in the N terminus of mature polypeptide chain: Ala for Arg(+1) and Gln for Glu(+4); Gln for Glu(+4). Enzyme activity was observed in all E. coli strains transformed by plasmids with cloned mutant genes. In addition, an amber mutation was introduced into the Arg(+1) position, and the synthesis of mutant alkaline phosphatase was shown in E. coli strains containing suppressor tRNAs specific for Ser, Gln, Tyr, Leu, Ala, Glu, Phe, Gly, His, Pro, and Cys.
AB - Various mutations in E. coli alkaline phosphatase gene were obtained by oligonucleotide-directed mutagenesis. They result in amino acid substitutions in the signal peptide cleavage site [Val for Ala(-1)] and in the N terminus of mature polypeptide chain: Ala for Arg(+1) and Gln for Glu(+4); Gln for Glu(+4). Enzyme activity was observed in all E. coli strains transformed by plasmids with cloned mutant genes. In addition, an amber mutation was introduced into the Arg(+1) position, and the synthesis of mutant alkaline phosphatase was shown in E. coli strains containing suppressor tRNAs specific for Ser, Gln, Tyr, Leu, Ala, Glu, Phe, Gly, His, Pro, and Cys.
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M3 - Article
C2 - 8145743
AN - SCOPUS:0028282763
SN - 0026-8984
VL - 28
SP - 150
EP - 157
JO - Molekulyarnaya Biologiya
JF - Molekulyarnaya Biologiya
IS - 1
ER -