scholarly journals Measuring Ultra-Weak Protein Self-Association by Non-ideal Sedimentation Velocity

2019 ◽  
Vol 141 (7) ◽  
pp. 2990-2996 ◽  
Author(s):  
Sumit K. Chaturvedi ◽  
Vatsala Sagar ◽  
Huaying Zhao ◽  
Graeme Wistow ◽  
Peter Schuck
Keyword(s):  
Sedimentation Velocity ◽  
Self Association

scholarly journals Quantitative Analysis of Protein Self‐Association by Sedimentation Velocity

2020 ◽  
Vol 101 (1) ◽  
Author(s):  
Huaying Zhao ◽  
Wenqi Li ◽  
Wendan Chu ◽  
Mary Bollard ◽  
Regina Adão ◽  
...  
Keyword(s):  
Quantitative Analysis ◽  
Sedimentation Velocity ◽  
Self Association

scholarly journals Solution behaviour of Chromobacter viscosum and Pseudomonas sp. lipases. No evidence of self-association

1991 ◽  
Vol 273 (3) ◽  
pp. 611-613 ◽  
Author(s):  
N J Simpkin ◽  
S E Harding ◽  
M P Tombs
Keyword(s):  
Sedimentation Velocity ◽  
Sedimentation Equilibrium ◽  
Pseudomonas Sp ◽  
Velocity Measurements ◽  
Absolute Determination ◽  
Sds Page ◽  
Self Association ◽  
Solution Behaviour

1. The size of two bacterial lipases was studied by SDS/PAGE, sedimentation velocity and sedimentation equilibrium to test for possible self-association behaviour. 2. Mr values of selected lipases were obtained from SDS/PAGE and sedimentation-velocity measurements, together with an absolute determination by sedimentation equilibrium 3. The Mr values obtained in a variety of aqueous solvents indicate that lipases do not self-associate in solution, suggesting the absence of surface hydrophobic patches.

Sedimentation velocity studies of the vinca-alkaloid-induced self-association of tubulin

1997 ◽  
Author(s):  
John J. Correia ◽  
Sharon Lobert ◽  
Anthony Frankfurter ◽  
Coleman A. Boyd ◽  
Bojana Vulevic
Keyword(s):  
Vinca Alkaloid ◽  
Sedimentation Velocity ◽  
Self Association

scholarly journals Self-association of proteoglycan subunits from pig laryngeal cartilage

1978 ◽  
Vol 171 (1) ◽  
pp. 109-114 ◽  
Author(s):  
J K Sheehan ◽  
I A Nieduszynski ◽  
C F Phelps
Keyword(s):  
Light Scattering ◽  
Ionic Strength ◽  
Guanidine Hydrochloride ◽  
Sedimentation Velocity ◽  
Dilute Solution ◽  
Thiol Groups ◽  
Dimer Model ◽  
Laryngeal Cartilage ◽  
Self Association ◽  
Corroborative Evidence

Proteoglycans from pig laryngeal cartilage prepared by dissociative extraction in guanidine hydrochloride were studied in dilute solution by light-scattering and ultracentrifugation. In buffered 150mM-NaCl, pH7.4, the proteoglycan particle weights were about 5×10(6) daltons, but at 100mM-, 200mM- and 300mM-NaCl particle weights of 2.5×10(6)–3.0×10(6) daltons were observed. These results, together with corroborative evidence from sedimentation-velocity experiments, were interpreted in terms of proteoglycans self-associating at physiological ionic strength. The data were examined by using a proteoglycan monomer-dimer model. Proteoglycan preparations that had thiol groups partially carboxymethylated gave particle weights of 3.2×10(6)–3.5×10(6) daltons in 150mM-NaCl, which suggested that carboxymethylation inhibited multimerization and hence that the protein core is implicated in the binding site. Further studies showed that the multimers were stable to 60 degrees C, unlike the hyaluronate-proteoglycan complex.

scholarly journals Investigating High Affinity Protein Self-Association by Fluorescence Optical Sedimentation Velocity Analytical Ultracentrifugation

2014 ◽  
Vol 106 (2) ◽  
pp. 151a
Author(s):  
Suvendu Lomash ◽  
Huaying Zhao ◽  
Carla Glasser ◽  
Mark L. Mayer ◽  
Peter Schuck
Keyword(s):  
Analytical Ultracentrifugation ◽  
Sedimentation Velocity ◽  
High Affinity ◽  
Self Association

scholarly journals Sedimentation Velocity Analysis of Flexible Macromolecules: Self-Association and Tangling of Amyloid Fibrils

2003 ◽  
Vol 84 (4) ◽  
pp. 2562-2569 ◽  
Author(s):  
Christopher A. MacRaild ◽  
Danny M. Hatters ◽  
Lynne J. Lawrence ◽  
Geoffrey J. Howlett
Keyword(s):  
Amyloid Fibrils ◽  
Sedimentation Velocity ◽  
Velocity Analysis ◽  
Self Association

scholarly journals Determination of the SLAMF1 self-association affinity constant with sedimentation velocity ultracentrifugation

2021 ◽  
pp. 114410
Author(s):  
Yangjie Wei ◽  
JangEun Lee ◽  
Michael Dziegelewski ◽  
Michael S. Marlow ◽  
David B. Hayes
Keyword(s):  
Sedimentation Velocity ◽  
Affinity Constant ◽  
Self Association
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