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Urease oligomerizes in a linear pattern: Further hydrodynamic evidence from intrinsic viscosity theories and measurement
Author(s) -
Tirrell Matthew,
Middleman Stanley
Publication year - 1979
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1979.360180107
Subject(s) - chemistry , intrinsic viscosity , viscosity , context (archaeology) , urease , monomer , thermodynamics , chemical physics , computational chemistry , polymer , enzyme , biochemistry , organic chemistry , physics , paleontology , biology
Measurements of the intrinsic viscosity of the urease “monomer” and of a mixture of oligomers are shown to lead to the conclusion that urease oligomerizes in a linear fashion, when viewed in the light of several available theories of intrinsic viscosity of rigid protein macromolecules. This conclusion is also consistent with previously reported work on the sedimentation coefficients of the urease oligomers. The use of a detailed subunit structure for the urease “monomer” and oligomers is explored and found to give quantitatively good results for all hydrodynamic properties of all urease oligomers. The realm of validity of the intrinsic viscosity theories proposed by Garcia de la Torre and Bloomfield, by Tsuda, and by Abdel‐Khalik and Bird is explored in this context.