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The macromolecular state of A‐kinase anchoring protein
Author(s) -
Patel Trushar R.,
Winzor Donald J.
Publication year - 2012
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.1164
Subject(s) - anchoring , size exclusion chromatography , oligomer , macromolecule , chemistry , globular protein , allowance (engineering) , chromatography , enzyme , biochemistry , polymer chemistry , economics , operations management , structural engineering , engineering
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. Copyright © 2011 John Wiley & Sons, Ltd.