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The conditions of digestion of colicin E3 with trypsin were examined to obtain an active fragment (T2A) of colicin E3, and a method suitable for large-scale preparation of T2A was developed. The T2A preparation thus obtained was homogeneous on SDS-polyacrylamide gel electrophoresis and the molecular weight was estimated to be about 11,000. T2A was composed of 97 amino acid residues and was rich in basic amino acids; methionine, valine, cysteine, and cystine were absent. The N-terminal residue was lysine and the structure near the C-terminus was -Lys-Lys-Tyr-Leu. Since T2A had no lysine or arginine residue at the C-terminus and since the C-terminal structure was identical to that of protein A, it was concluded that T2A was derived from the C-terminal region of protein A. No clear differences were detected among T2A preparations obtained from 3 different fractions of colicin E3, suggesting that the apparent homogeneity of colicin E3 does not involve the T2A region.
K Suzuki, and
K Imahori
November 1967,
The Journal of biological chemistry,
K Suzuki, and
K Imahori
November 1982,
FEBS letters,
K Suzuki, and
K Imahori
March 1978,
Journal of biochemistry,
K Suzuki, and
K Imahori
June 1979,
Journal of bacteriology,
K Suzuki, and
K Imahori
January 1976,
Seikagaku. The Journal of Japanese Biochemical Society,
K Suzuki, and
K Imahori
June 1979,
Zentralblatt fur Bakteriologie, Parasitenkunde, Infektionskrankheiten und Hygiene. Erste Abteilung Originale. Reihe A: Medizinische Mikrobiologie und Parasitologie,
K Suzuki, and
K Imahori
November 1993,
Molecular and cellular biochemistry,
K Suzuki, and
K Imahori
March 1985,
Journal of molecular biology,
K Suzuki, and
K Imahori
January 1973,
Proceedings of the National Academy of Sciences of the United States of America,
