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Denaturation of globular proteins. Interaction of guanidinium salts with three proteins

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    Denaturation of globular proteins. Interaction of guanidinium salts with three proteins
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    Biochemistry

    Cite this: Biochemistry 1972, 11, 10, 1862–1870
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    https://doi.org/10.1021/bi00760a021
    Published May 9, 1972
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    1. Laura B. Sagle, Yanjie Zhang, Vladislav A. Litosh, Xin Chen, Younhee Cho and Paul S. Cremer. Investigating the Hydrogen-Bonding Model of Urea Denaturation. Journal of the American Chemical Society 2009, 131 (26) , 9304-9310. https://doi.org/10.1021/ja9016057
    2. Nihar Nalini Mohanty, Vikas Gupta, Laxmi Narayan Sarangi, Rohini Bhat, Sathish B. Shivachandra. Protocols for Isolation of Genetic Materials from RNA Viruses. 2022, 49-66. https://doi.org/10.1007/978-1-0716-2043-4_4
    3. Serena Cozzolino, Attila Tortorella, Pompea Del Vecchio, Giuseppe Graziano. General Counteraction Exerted by Sugars against Denaturants. Life 2021, 11 (7) , 652. https://doi.org/10.3390/life11070652
    4. Michael R. Green, Joseph Sambrook. Isolation of Total RNA Using Monophasic Lysis Reagents. Cold Spring Harbor Protocols 2020, 2020 (9) , pdb.top101642. https://doi.org/10.1101/pdb.top101642
    5. Claudio Asencio, Aindrila Chatterjee, Matthias W Hentze. Silica-based solid-phase extraction of cross-linked nucleic acid–bound proteins. Life Science Alliance 2018, 1 (3) , e201800088. https://doi.org/10.26508/lsa.201800088
    6. Felix Ameseder, Aurel Radulescu, Marina Khaneft, Wiebke Lohstroh, Andreas M. Stadler. Homogeneous and heterogeneous dynamics in native and denatured bovine serum albumin. Physical Chemistry Chemical Physics 2018, 20 (7) , 5128-5139. https://doi.org/10.1039/C7CP08292D
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    17. G. Unterhaslberger, C. Schmitt, C. Sanchez, C. Appolonia-Nouzille, A. Raemy. Heat denaturation and aggregation of β-lactoglobulin enriched WPI in the presence of arginine HCl, NaCl and guanidinium HCl at pH 4.0 and 7.0. Food Hydrocolloids 2006, 20 (7) , 1006-1019. https://doi.org/10.1016/j.foodhyd.2005.10.017
    18. Emilia Bramanti, Chiara Allegrini, Massimo Onor, Giorgio Raspi, Kristen J. Skogerboe, Robert E. Synovec. Flow injection analysis with diode array absorbance detection and dynamic surface tension detection for studying denaturation and surface activity of globular proteins. Analytical Biochemistry 2006, 351 (1) , 100-113. https://doi.org/10.1016/j.ab.2005.12.017
    19. Robert E. Farrell. RNA Isolation Strategies. 2005, 67-113. https://doi.org/10.1016/B978-012249696-7/50005-6
    20. Roman Kotlowski, Anandi Martin, Anthony Ablordey, Karim Chemlal, Pierre-Alain Fonteyne, Françoise Portaels. One-tube cell lysis and DNA extraction procedure for PCR-based detection of Mycobacterium ulcerans in aquatic insects, molluscs and fish. Journal of Medical Microbiology 2004, 53 (9) , 927-933. https://doi.org/10.1099/jmm.0.45593-0
    21. Emilia Bramanti, Chandra Sortino, Cristina Lomonte, Massimo Onor, Roberto Zamboni, Giorgio Raspi, Alessandro D’Ulivo. Hydrophobic interaction chromatography coupled with atomic fluorescence spectrometric detection. Talanta 2004, 63 (2) , 383-389. https://doi.org/10.1016/j.talanta.2003.11.002
    22. Emilia Bramanti, Fabrizio Ferri, Chandra Sortino, Massimo Onor, Giorgio Raspi, Marcella Venturini. Characterization of denatured proteins by hydrophobic interaction chromatography: A preliminary study. Biopolymers 2003, 69 (3) , 293-300. https://doi.org/10.1002/bip.10366
    23. Ali Ahmed Alsallami, Roman Kotłowski. Selection of primers for specific detection of Clostridium botulinum types B and E neurotoxin genes using PCR method. International Journal of Food Microbiology 2001, 69 (3) , 247-253. https://doi.org/10.1016/S0168-1605(01)00499-8
    24. C.L Kho, M.L Mohd-Azmi, S.S Arshad, K Yusoff. Performance of an RT-nested PCR ELISA for detection of Newcastle disease virus. Journal of Virological Methods 2000, 86 (1) , 71-83. https://doi.org/10.1016/S0166-0934(99)00185-8
    25. Gregory T. DeKoster, Andrew D. Robertson. Calorimetrically-derived parameters for protein interactions with urea and guanidine-HCl are not consistent with denaturant m values. Biophysical Chemistry 1997, 64 (1-3) , 59-68. https://doi.org/10.1016/S0301-4622(96)02219-3
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    50. Detlef Gabel. The Denaturation by Urea and Guanidinium Chloride of Trypsin and N ‐Acetylated‐Trypsin Derivatives Bound to Sephadex and Agarose. European Journal of Biochemistry 1973, 33 (2) , 348-356. https://doi.org/10.1111/j.1432-1033.1973.tb02689.x
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    Biochemistry

    Cite this: Biochemistry 1972, 11, 10, 1862–1870
    Click to copy citationCitation copied!
    https://doi.org/10.1021/bi00760a021
    Published May 9, 1972
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