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B.F. Parten J.C. Anders (2003)
Using amino acid analysis to determine absorptivity constants: A validation case study using bovine serum albuminBioPharm Int., 2
G. Sittampalam, R. Ellis, D. Miner, E. Rickard, D. Clodfelter (1988)
Evaluation of amino acid analysis as reference method to quantitate highly purified proteins.Journal - Association of Official Analytical Chemists, 71 4
S. Gill, Von Hippel (1989)
Calculation of protein extinction coefficients from amino acid sequence data.Analytical biochemistry, 182 2
O. Lowry, N. Rosebrough, A. Farr, R. Randall (1951)
Protein measurement with the Folin phenol reagent.The Journal of biological chemistry, 193 1
E. Layne (1957)
SPECTROPHOTOMETRIC AND TURBIDIMETRIC METHODS FOR MEASURING PROTEINSMethods in Enzymology, 3
Katharina Diepold, Katrin Bomans, M. Wiedmann, B. Zimmermann, A. Petzold, Tilman Schlothauer, R. Mueller, Bernd Moritz, J. Stracke, Michael Mølhøj, D. Reusch, Patrick Bulau (2012)
Simultaneous Assessment of Asp Isomerization and Asn Deamidation in Recombinant Antibodies by LC-MS following Incubation at Elevated TemperaturesPLoS ONE, 7
(1942)
Insulation and crystalisation of the Fermenting process of enolase
C.N. Pace G.R. Grimsley (2004)
Spectrophotometric determination of protein concentrationCurr. Protoc. Protein Sci, 33
M. Bradford (1976)
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.Analytical biochemistry, 72
S. Rutherfurd, B. Dunn (1995)
Quantitative Amino Acid AnalysisCurrent Protocols in Protein Science, 63
Philippe Desjardins, J. Hansen, Michael Allen (2009)
Microvolume Spectrophotometric and Fluorometric Determination of Protein ConcentrationCurrent Protocols in Protein Science, 55
F. Greer (2002)
Greer, F., Reason, A. & Rogers, M. Post-translational modifications of biopharmaceuticals-a challenge for analytical characterisation. European BioPharm. Rev. 106-111 (2002).
C. Pace, F. Vajdos, L. Fee, G. Grimsley, Theronica Gray (1995)
How to measure and predict the molar absorption coefficient of a proteinProtein Science, 4
Jae-Young Byeon, Yoo-Joo Choi, J. Suh (2015)
Structural Characterization of Modification on the Interface between a Ligand and its Receptor for BiopharmaceuticalsReceptors and clinical investigation, 2
M. Simonian (2002)
Spectrophotometric Determination of Protein ConcentrationCurrent Protocols in Toxicology, 21
J. Anders, B. Parten, G. Petrie, R. Marlowe, J. McEntire (2003)
A Validation Case Study Using Bovine Serum Albumin
(1997)
How to determine the molar absorbance coefficient of a protein
J. Anders, B. Parten, G. Petrie, R. Marlowe, J. McEntire (2003)
Using Amino Acid Analysis to Determine Absorptivity Constants
B. Dunn (2006)
Quantitative amino acid analysisCurr. Protoc. Mol. Biol., 76
Kwang-Eun Song, Jae-Young Byeon, D. Moon, Hyong-Ha Kim, Yoo-Joo Choi, J. Suh (2014)
Structural Identification of Modified Amino Acids on the Interface between EPO and Its Receptor from EPO BRP, Human Recombinant Erythropoietin by LC/MS AnalysisMolecules and Cells, 37
J. Ozols (1990)
Amino acid analysis.Methods in enzymology, 182
G. Walsh (2009)
Post-translational modifications of protein biopharmaceuticals.Drug discovery today, 15 17-18
(2002)
Post-translational modifications of biopharmaceuticals-a challenge for analytical characterisation
Abstract Spectrophotometric procedure is a traditional method for quantifying protein concentration in solution. The benefit of this method is simple and direct, not requiring standard materials, sample incubation, and exogenous chromophore addition. There are also some drawbacks, low detection limits and high amounts of protein needed. The recent advances in fiber optics and nano-technology enable to overcome those drawbacks by using microvolume sampling and extremely short pathlengths. In this study, the utility of the microvolume system with microfluidic carriers was assessed for concentration measurement of biopharmaceutical protein using absorbance at 280 nm and also compared to a traditional instrument. The results show a high correlation of estimation by Cohen’s d effect size and Pearson correlation coefficient between two different spectrometers. For UV spectral analysis, there are no statistically significant difference between those spectra from a microvolume spectrometer and a traditional one. For the extinction coefficient determination, two different spectrometers also give quite comparable and similar values. Thus a microvolume spectrometer can be used as an alternative over a traditional one to determine the concentration of biopharmaceutical protein. Moreover, the dynamic range for protein quantification by a microvolume spectrometer is over 10-fold higher than that of a traditional one.
BioChip Journal – Springer Journals
Published: Mar 1, 2017
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