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Incubate at 23 °C (73 °F) for 20 minutes; Centrifuge for 20 minutes at 16,000 G at 23 °C (73 °F) Invert filter and spin for 3 minutes at 2000 G; Bring the sample back to a neutral pH with 15-2uL 2.5M Tris pH9; Add ELISA buffer (1.5% BSA and 0.05% Tween 20 in phosphate buffered saline) Perform ELISA analysis.
In cell biology, protein kinase A (PKA) is a family of serine-threonine kinase [1] whose activity is dependent on cellular levels of cyclic AMP (cAMP). PKA is also known as cAMP-dependent protein kinase (EC 2.7.11.11). PKA has several functions in the cell, including regulation of glycogen, sugar, and lipid metabolism.
The G s alpha subunit slowly catalyzes the hydrolysis of GTP to GDP, which in turn deactivates the G s protein, shutting off the cAMP pathway. The pathway may also be deactivated downstream by directly inhibiting adenylyl cyclase or dephosphorylating the proteins phosphorylated by PKA. Molecules that inhibit the cAMP pathway include:
The normal function of Aβ is not yet known. [9] Though some animal studies have shown that the absence of Aβ does not lead to any obvious loss of physiological function, [10] [11] several potential activities have been discovered for Aβ, including activation of kinase enzymes, [12] [13] protection against oxidative stress, [14] [15] regulation of cholesterol transport, [16] [17] functioning ...
The biochemistry of Alzheimer's disease, the most common cause of dementia, is not yet very well understood. Alzheimer's disease (AD) has been identified as a proteopathy : a protein misfolding disease due to the accumulation of abnormally folded amyloid beta (Aβ) protein in the brain . [ 1 ]
Edmond H. Fischer and Edwin G. Krebs at the University of Washington discovered PKA in the late 1950s while working through the mechanisms that govern glycogen phosphorylase. They realized that a key metabolic enzyme called phosphorylase kinase was activated by another kinase that was dependent on the second messenger cyclic AMP (cAMP). [ 9 ]
From the titration of protonatable group, one can read the so-called pK a 1 ⁄ 2 which is equal to the pH value where the group is half-protonated (i.e. when 50% such groups would be protonated). The p K a 1 ⁄ 2 is equal to the Henderson–Hasselbalch p K a (p K HH
The A-kinase anchor proteins (AKAPs) are a group of structurally diverse proteins that have the common function of binding to the regulatory subunit of protein kinase A (PKA) and confining the holoenzyme to discrete locations within the cell. This gene encodes a member of the AKAP family.
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