-transparent.png){kind=logo}
An inhibitor protein of the catalytic subunit of the cyclic 3',5'-AMP-dependent protein kinase from the nematode Ascaris suum was isolated and characterized. The molecular weight of the inhibitor was estimated as 28,000 by electrophoresis under denaturing conditions and as 30,000 by gel permeation chromatography on Superose 12. The Trypsin-labile inhibitor was resistant to short incubations (less than or equal to 5 min) at temperatures up to 95 degrees C and at pH 3. It affected the protein kinase from Ascaris and bovine heart with almost the same affinity, and inhibition was not relieved by the presence of cAMP and cGMP. However, the inhibition was antagonized by low concentrations of heparin. Unlike in mammalian tissues, the concentration of the inhibitor was sufficiently high to exert at least 90% inhibition of the protein kinase activity in Ascaris muscle. Therefore, the inhibitor may play a role in cellular regulation in the nematode.
R Hoffmann, and
S Jung, and
H W Hofer
September 1989,
Archives of biochemistry and biophysics,
R Hoffmann, and
S Jung, and
H W Hofer
June 1989,
Archives of biochemistry and biophysics,
R Hoffmann, and
S Jung, and
H W Hofer
October 1976,
Biochemical and biophysical research communications,
R Hoffmann, and
S Jung, and
H W Hofer
November 1976,
Proceedings of the National Academy of Sciences of the United States of America,
R Hoffmann, and
S Jung, and
H W Hofer
March 1977,
Journal of neurochemistry,
R Hoffmann, and
S Jung, and
H W Hofer
January 1978,
Biochimie,
R Hoffmann, and
S Jung, and
H W Hofer
June 1986,
Biochemistry,
R Hoffmann, and
S Jung, and
H W Hofer
March 1979,
Biochimica et biophysica acta,
R Hoffmann, and
S Jung, and
H W Hofer
January 1974,
Methods in enzymology,
R Hoffmann, and
S Jung, and
H W Hofer
January 1998,
Advances in experimental medicine and biology,
