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A proteinous fraction that produces endothelin-1 (ET-1) from big ET-1 in guinea-pig lung cytosol is described. An active protein has been successfully purified to homogeneity by combinations of sequential column chromatographies. The purified enzyme was a metalloenzyme based upon its sensitivity to chelating agent, and a molecular mass of the enzyme was 38 kDa estimated by gel filtration and SDS-PAGE. Further investigations revealed that the enzyme activity was abolished by sulfhydryl modifier such as N-ethylmaleimide, but inhibited neither by phosphoramidon, by thiorphan nor by captopril. The enzyme actually produced ET-1 with the Km value of 14.5 microM for big ET-1. These results indicate that this enzyme seems to be a novel metalloprotease that converts big ET-1 to ET-1.
H Shima, and
M Yamanouchi, and
K Omori, and
M Sugiura
December 1994,
Biochemistry and molecular biology international,
H Shima, and
M Yamanouchi, and
K Omori, and
M Sugiura
May 1998,
FEBS letters,
H Shima, and
M Yamanouchi, and
K Omori, and
M Sugiura
April 1990,
Journal of pharmacological methods,
H Shima, and
M Yamanouchi, and
K Omori, and
M Sugiura
January 1995,
Biochemical pharmacology,
H Shima, and
M Yamanouchi, and
K Omori, and
M Sugiura
January 1995,
Journal of cardiovascular pharmacology,
H Shima, and
M Yamanouchi, and
K Omori, and
M Sugiura
April 1995,
British journal of pharmacology,
H Shima, and
M Yamanouchi, and
K Omori, and
M Sugiura
September 1982,
Archives of biochemistry and biophysics,
H Shima, and
M Yamanouchi, and
K Omori, and
M Sugiura
November 1994,
Analytical biochemistry,
H Shima, and
M Yamanouchi, and
K Omori, and
M Sugiura
October 1993,
The Journal of biological chemistry,
H Shima, and
M Yamanouchi, and
K Omori, and
M Sugiura
January 1991,
Journal of cardiovascular pharmacology,
