The macromolecular state of A-kinase anchoring protein.
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.
Department of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada, R3T 2N2. patelt@cc.manitoba.ca
Trushar R
TR
Patel
Donald J
DJ
Winzor
D054758:A Kinase Anchor Proteins / Q000032:analysis* / Q000737:chemistry*; D002850:Chromatography, Gel / Q000379:methods*; D046911:Macromolecular Substances / Q000737:chemistry / Q000378:metabolism; D008970:Molecular Weight
D054758:A Kinase Anchor Proteins; D046911:Macromolecular Substances