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Activation of sterol ester hydrolase of bovine corpus luteum by N 6 ,O 2′ ‐dibutyryl cyclic adenosine 3′∶5′‐phosphate
Author(s) -
Bisgaier Charles L.,
Treadwell C. R.,
Vahouny V.
Publication year - 1979
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02533557
Subject(s) - corpus luteum , sterol , enzyme , adenosine , chemistry , homogenization (climate) , hydrolase , protein kinase a , biochemistry , medicine , endocrinology , biology , hormone , cholesterol , biodiversity , ecology
The direct activation of sterol ester hydrolase (E.C. 3.1.1.13) in homogenates of bovine corpus luteum by N 6 O 2′ ·dibutyryl cyclic adenosine 3′∶5′‐phosphate, (dibutyryl cAMP), adenosine triphosphate (ATP), and Mg 2+ has been demonstrated. Variability in the extent of activation by the additions was minimized by homogenization of the tissue in 5 mM Mg 2+ . Baseline sterol ester hydrolase activity was primarily associated with the 105,000 × g soluble fraction, and significant activation of the enzyme preparation preincubated with dibutyryl cAMP, ATP and Mg 2+ occurred within the first 15 min, prior to addition of substrate. A requirement for protein kinase in the system was demonstrated by blocking the cofactor‐dependent enzyme activation with commercial protein kinase inhibitor.