Related Experiment Video
Updated: May 26, 2026

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
Published on: June 30, 2019
The macromolecular state of A-kinase anchoring protein
Trushar R Patel1, Donald J Winzor
1Department of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada, R3T 2N2. patelt@cc.manitoba.ca
Abstract:
The amendment of the interpretation of recently published size-exclusion chromatography (SEC) data for A-kinase anchoring protein (AKAP12) on Sephacryl-S400 has led to an increase in the estimated size of the supermolecular state from 840 to at least 6000 kDa. Although size-exclusion chromatography has sufficed to demonstrate unequivocally the existence of this 190-kDa scaffold protein in a supermolecular state, any quantitative estimate of the oligomer stoichiometry is shown to be precluded by failure of this empirical procedure to incorporate allowance for any deviation from globular shape--an important consideration in view of the extended structures exhibited by other extracellular matrix proteins.
Related Concept Videos
Lipids as Anchors
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...
Assembly of Signaling Complexes
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Protein Kinases and Phosphatases
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Kinases and Phosphatases
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Calmodulin-dependent Signaling
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Amplifying Signals via Enzymatic Cascade

