Acknowledgments
The authors would like to thank Margarida Bastos for helpful
comments on the manuscript.
References
1. Noble JE (2014) Quantification of protein
concentration using UV absorbance and Coomassie dyes. Methods Enzymol 536:17–26.
https://doi.org/10.1016/B978-0-12420070-8.00002-7
2. Noble JE, Bailey MJA (2009) Chapter 8 Quantitation of protein. Methods Enzymol
463:73–95.
https://doi.org/10.1016/
S0076-6879(09)63008-1
3. Raynal B, Lenormand P, Baron B, Hoos S,
England P (2014) Quality assessment and optimization of purified protein samples: why and
how? Microb Cell Factories 13:180. https://
doi.org/10.1186/s12934-014-0180-6
4. Pace CN, Vajdos F, Fee L, Grimsley G, Gray T
(1995) How to measure and predict the molar
absorption coefficient of a protein. Protein Sci
4:2411–2423. https://doi.org/10.1002/pro.
5560041120
5. Glasel J (1995) Validity of nucleic acid purities
monitored by 260nm/280nm absorbance
ratios. BioTechniques 18:62–63
6. Andrews AT (1986) Electrophoresis: theory,
techniques and biochemical and clinical applications. Clarendon Press, Oxford
7. Rothe GM (1994) Electrophoresis of enzymes.
In: Laboratory methods. Springer, Berlin
8. Laemmli UK (1970) Cleavage of structural
proteins during the assembly of the head of
bacteriophage T4. Nature 227:680–685.
https://doi.org/10.1038/227680a0
9. Krause F (2006) Detection and analysis of
protein-protein interactions in organellar and
prokaryotic proteomes by native gel electrophoresis: (Membrane) protein complexes and
supercomplexes.
Electrophoresis
27:2759–2781.
https://doi.org/10.1002/
elps.200600049
10. Sch€ agger H, von Jagow G (1991) Blue native
electrophoresis for isolation of membrane protein complexes in enzymatically active form.
Anal Biochem 199:223–231. https://doi.
org/10.1016/0003-2697(91)90094-a
11. Nobbmann U, Connah M, Fish B, Varley P,
Gee C, Mulot S, Chen J, Zhou L, Lu Y, Shen F,
Yi J, Harding SE (2007) Dynamic light scattering as a relative tool for assessing the molecular
integrity and stability of monoclonal
antibodies. Biotechnol Genet Eng Rev
24:117–128.
https://doi.org/10.1080/
02648725.2007.10648095
12. Fekete S, Beck A, Veuthey J-L, Guillarme D
(2014) Theory and practice of size exclusion
chromatography for the analysis of protein
aggregates.
J
Pharm
Biomed
Anal
101:161–173.
https://doi.org/10.1016/j.
jpba.2014.04.011
13. Sahin E, Roberts CJ (2012) Size-exclusion
chromatography with multi-angle light scattering for elucidating protein aggregation
mechanisms. In: Voynov V, Caravella JA (eds)
Therapeutic proteins, vol 899. Springer
Nature, Cham, pp 403–423
14. Heck AJR, Van Den Heuvel RHH (2004)
Investigation of intact protein complexes by
mass spectrometry. Mass Spectrom Rev
23:368–389. https://doi.org/10.1002/mas.
10081
15. Fenn JB, Mann M, Meng CK, Wong SF,
Whitehouse CM (1989) Electrospray ionization for mass spectrometry of large biomolecules. Science 246:64–71. https://doi.org/10.
1126/science.2675315
16. Tanaka K, Waki H, Ido Y, Akita S, Yoshida Y
(1988) Protein and polymer analyses up to m/
z 100 000 by laser ionization time-of-flight
mass spectrometry. Rapid Commun Mass
Spectrom 2:151–153. https://doi.org/10.
1002/rcm.1290020802
17. Eakin CM, Miller A, Kerr J, Kung J, Wallace A
(2014) Assessing analytical methods to monitor isoAsp formation in monoclonal antibodies. Front Pharmacol 5:87. https://doi.org/
10.3389/fphar.2014.00087
18. Daviter T, Chmel N, Rodger A (2013) Circular
and linear dichroism spectroscopy for the study
of protein-ligand interactions. In: Williams M,
Daviter T (eds) Protein-ligand interactions:
methods and applications. Humana Press,
Totowa, NJ, pp 211–241
19. Greenfield NJ (2006) Using circular dichroism
collected as a function of temperature to determine the thermodynamics of protein unfolding
and binding interactions. Nat Protoc
1:2527–2535.
https://doi.org/10.1038/
nprot.2006.204
44
Bertrand Raynal et al.
The authors would like to thank Margarida Bastos for helpful
comments on the manuscript.
References
1. Noble JE (2014) Quantification of protein
concentration using UV absorbance and Coomassie dyes. Methods Enzymol 536:17–26.
https://doi.org/10.1016/B978-0-12420070-8.00002-7
2. Noble JE, Bailey MJA (2009) Chapter 8 Quantitation of protein. Methods Enzymol
463:73–95.
https://doi.org/10.1016/
S0076-6879(09)63008-1
3. Raynal B, Lenormand P, Baron B, Hoos S,
England P (2014) Quality assessment and optimization of purified protein samples: why and
how? Microb Cell Factories 13:180. https://
doi.org/10.1186/s12934-014-0180-6
4. Pace CN, Vajdos F, Fee L, Grimsley G, Gray T
(1995) How to measure and predict the molar
absorption coefficient of a protein. Protein Sci
4:2411–2423. https://doi.org/10.1002/pro.
5560041120
5. Glasel J (1995) Validity of nucleic acid purities
monitored by 260nm/280nm absorbance
ratios. BioTechniques 18:62–63
6. Andrews AT (1986) Electrophoresis: theory,
techniques and biochemical and clinical applications. Clarendon Press, Oxford
7. Rothe GM (1994) Electrophoresis of enzymes.
In: Laboratory methods. Springer, Berlin
8. Laemmli UK (1970) Cleavage of structural
proteins during the assembly of the head of
bacteriophage T4. Nature 227:680–685.
https://doi.org/10.1038/227680a0
9. Krause F (2006) Detection and analysis of
protein-protein interactions in organellar and
prokaryotic proteomes by native gel electrophoresis: (Membrane) protein complexes and
supercomplexes.
Electrophoresis
27:2759–2781.
https://doi.org/10.1002/
elps.200600049
10. Sch€ agger H, von Jagow G (1991) Blue native
electrophoresis for isolation of membrane protein complexes in enzymatically active form.
Anal Biochem 199:223–231. https://doi.
org/10.1016/0003-2697(91)90094-a
11. Nobbmann U, Connah M, Fish B, Varley P,
Gee C, Mulot S, Chen J, Zhou L, Lu Y, Shen F,
Yi J, Harding SE (2007) Dynamic light scattering as a relative tool for assessing the molecular
integrity and stability of monoclonal
antibodies. Biotechnol Genet Eng Rev
24:117–128.
https://doi.org/10.1080/
02648725.2007.10648095
12. Fekete S, Beck A, Veuthey J-L, Guillarme D
(2014) Theory and practice of size exclusion
chromatography for the analysis of protein
aggregates.
J
Pharm
Biomed
Anal
101:161–173.
https://doi.org/10.1016/j.
jpba.2014.04.011
13. Sahin E, Roberts CJ (2012) Size-exclusion
chromatography with multi-angle light scattering for elucidating protein aggregation
mechanisms. In: Voynov V, Caravella JA (eds)
Therapeutic proteins, vol 899. Springer
Nature, Cham, pp 403–423
14. Heck AJR, Van Den Heuvel RHH (2004)
Investigation of intact protein complexes by
mass spectrometry. Mass Spectrom Rev
23:368–389. https://doi.org/10.1002/mas.
10081
15. Fenn JB, Mann M, Meng CK, Wong SF,
Whitehouse CM (1989) Electrospray ionization for mass spectrometry of large biomolecules. Science 246:64–71. https://doi.org/10.
1126/science.2675315
16. Tanaka K, Waki H, Ido Y, Akita S, Yoshida Y
(1988) Protein and polymer analyses up to m/
z 100 000 by laser ionization time-of-flight
mass spectrometry. Rapid Commun Mass
Spectrom 2:151–153. https://doi.org/10.
1002/rcm.1290020802
17. Eakin CM, Miller A, Kerr J, Kung J, Wallace A
(2014) Assessing analytical methods to monitor isoAsp formation in monoclonal antibodies. Front Pharmacol 5:87. https://doi.org/
10.3389/fphar.2014.00087
18. Daviter T, Chmel N, Rodger A (2013) Circular
and linear dichroism spectroscopy for the study
of protein-ligand interactions. In: Williams M,
Daviter T (eds) Protein-ligand interactions:
methods and applications. Humana Press,
Totowa, NJ, pp 211–241
19. Greenfield NJ (2006) Using circular dichroism
collected as a function of temperature to determine the thermodynamics of protein unfolding
and binding interactions. Nat Protoc
1:2527–2535.
https://doi.org/10.1038/
nprot.2006.204
44
Bertrand Raynal et al.