-transparent.png){kind=logo}
Escherichia coli harboring the gene coding for human interleukin-2 (IL-2) produced methionyl IL-2 (Met-IL-2) having an additional methionine residue at the amino terminus as well as IL-2 starting with the amino terminal alanine. IL-2 and Met-IL-2 were copurified from a cell-free extract. It was difficult to separate these two molecular species from each other because of the similarities of their physico-chemical characteristics. We found that the isoelectric points of IL-2 and Met-IL-2 were slightly but significantly different and succeeded in separating these two molecular species by utilizing the difference of their isoelectric points. The isoelectric points of IL-2 and Met-IL-2 thus obtained were determined to be 7.7 and 7.5, respectively. The in vitro specific activities of these two species were the same and similar to that of natural human IL-2 derived from peripheral blood lymphocytes.
T Yamada, and
K Kato, and
K Kawahara, and
O Nishimura
March 1984,
Science (New York, N.Y.),
T Yamada, and
K Kato, and
K Kawahara, and
O Nishimura
August 1987,
Biochemical and biophysical research communications,
T Yamada, and
K Kato, and
K Kawahara, and
O Nishimura
April 2010,
Biotechnology and applied biochemistry,
T Yamada, and
K Kato, and
K Kawahara, and
O Nishimura
July 1989,
Gene,
T Yamada, and
K Kato, and
K Kawahara, and
O Nishimura
June 1995,
Biochemical and biophysical research communications,
T Yamada, and
K Kato, and
K Kawahara, and
O Nishimura
January 2014,
Biotechnology and applied biochemistry,
T Yamada, and
K Kato, and
K Kawahara, and
O Nishimura
January 2013,
PloS one,
T Yamada, and
K Kato, and
K Kawahara, and
O Nishimura
February 1993,
Doklady Akademii nauk,
T Yamada, and
K Kato, and
K Kawahara, and
O Nishimura
May 2024,
Protein expression and purification,
T Yamada, and
K Kato, and
K Kawahara, and
O Nishimura
November 1991,
Applied microbiology and biotechnology,
