-transparent.png){kind=logo}
Insulin sensitive phosphodiesterase from rat adipocytes is found in particulate fractions. Solubilisation of the enzyme with triton X-100 yields a preparation containing more than one phosphodiesterase activity as judged by its rate of thermal denaturation at 45 degrees C and by its non-linear kinetic plots. Immunoprecipitation of solubilised activity with a polyclonal antiserum raised against purified insulin-sensitive rat liver phosphodiesterase selected a form of the enzyme which showed a single exponential decay of enzyme activity when heated at 45 degrees C and linear low Km kinetics. Treatment of adipocytes with insulin ACTH, glucagon or isoproterenol stimulated the low Km particulate phosphodiesterase. The hormonal activation was retained following solubilisation and was also seen when activity was immunoprecipitated. It is suggested that all four hormones activate the same form of phosphodiesterase.
S Boyes, and
E G Loten
January 1988,
Methods in enzymology,
S Boyes, and
E G Loten
June 1975,
Endocrinology,
S Boyes, and
E G Loten
May 1974,
Voprosy meditsinskoi khimii,
S Boyes, and
E G Loten
January 1970,
Hormone and metabolic research = Hormon- und Stoffwechselforschung = Hormones et metabolisme,
S Boyes, and
E G Loten
January 1972,
Verhandlungen der Deutschen Gesellschaft fur Innere Medizin,
S Boyes, and
E G Loten
November 1998,
Hormone and metabolic research = Hormon- und Stoffwechselforschung = Hormones et metabolisme,
S Boyes, and
E G Loten
October 1991,
Endocrinology,
S Boyes, and
E G Loten
May 1982,
The Journal of biological chemistry,
S Boyes, and
E G Loten
July 1950,
The Journal of biological chemistry,
S Boyes, and
E G Loten
February 1966,
The Journal of biological chemistry,
