-transparent.png){kind=logo}
Functionally active A and B chains were separated from a two-chain form of recombinant tissue-type plasminogen activator after mild reduction and alkylation. The A chain was found to be responsible for the binding to lysine-Sepharose or fibrin and the B chain contained the catalytic activity of tissue-type plasminogen activator. An extensive reduction of two-chain tissue-type plasminogen activator, however, destroyed both the binding and catalytic activities. A thermolytic fragment, Fr. 1, of tissue-type plasminogen activator that contained a growth factor and two kringle segments retained its lysine binding activity. Additional thermolytic cleavages in the kringle-2 segment of Fr. 1 caused a total loss of the binding activity. These results indicated that the binding site of tissue-type plasminogen activator to fibrin was located in the kringle-2 segment.
A Ichinose, and
K Takio, and
K Fujikawa
July 1996,
The Journal of biological chemistry,
A Ichinose, and
K Takio, and
K Fujikawa
August 1992,
The Journal of biological chemistry,
A Ichinose, and
K Takio, and
K Fujikawa
September 1989,
Biochemistry,
A Ichinose, and
K Takio, and
K Fujikawa
December 1987,
Biochimica et biophysica acta,
A Ichinose, and
K Takio, and
K Fujikawa
March 1998,
Blood,
A Ichinose, and
K Takio, and
K Fujikawa
January 1994,
Chemistry and physics of lipids,
A Ichinose, and
K Takio, and
K Fujikawa
May 1992,
Blood,
A Ichinose, and
K Takio, and
K Fujikawa
August 1991,
Biochemical and biophysical research communications,
A Ichinose, and
K Takio, and
K Fujikawa
January 1991,
Biomedica biochimica acta,
A Ichinose, and
K Takio, and
K Fujikawa
July 1993,
Protein engineering,
