Changes in structure of upon reaction with trypsin as assessed by light scattering and differential scanning calorimetry
作者： C.Russell Middaugh , Bryan L. Steadman , Peter Schurtenberger , Douglas C. Lee , Jan F. Chlebowski
DOI: 10.1016/0167-4838(93)90233-H
关键词: Analytical chemistry 、 Calorimetry 、 Differential scanning calorimetry 、 Light scattering 、 Chemistry 、 Radius of gyration 、 Molecule 、 Crystallography 、 Hydrodynamic radius 、 Trypsin 、 Dynamic light scattering
摘要: Abstract Employing a combination of static and dynamic light scattering, as well differential scanning calorimetry (DSC), the structural changes which appear in α 2 - macroglobulin ( M ) upon trypsin binding have been further characterized. Light-scattering measurements suggest that 15% reduction both hydrodynamic radius gyration occurs when two molecules complex to . Approx. 85% this trypsin-induced compaction results from first proteinase. A complementary was obtained DSC major fraction conversion single more thermally stable form interaction with proteinase molecule. These observations support functionally asymmetric model significant size is primarily due initial
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