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Avoiding Proteolysis During Protein Purification.

B. J. Ryan, G. Henehan
Published 2017 · Chemistry, Medicine

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All cells contain proteases which hydrolyze the peptide bonds between amino acids in a protein backbone. Typically, proteases are prevented from nonspecific proteolysis by regulation and by their physical separation into different subcellular compartments; however, this segregation is not retained during cell lysis, which is the initial step in any protein isolation procedure. Prevention of proteolysis during protein purification often takes the form of a two-pronged approach; firstly inhibition of proteolysis in situ, followed by the early separation of the protease from the protein of interest via chromatographical purification. Protease inhibitors are routinely used to limit the effect of the proteases before they are physically separated from the protein of interest via column chromatography. Here, commonly used approaches to reducing or avoiding proteolysis during protein purification and subsequent chromatography are reviewed.
This paper references
10.1016/0166-6851(94)90024-8
Sequence, expression and modeled structure of an aspartic proteinase from the human malaria parasite Plasmodium falciparum.
J. B. Dame (1994)
10.1038/nsmb.2203
New approaches for dissecting protease functions to improve probe development and drug discovery
Edgar Deu (2012)
10.1016/0076-6879(94)44004-2
[2] Families of serine peptidases
N. Rawlings (1994)
10.1016/J.JCHROMB.2006.10.040
Methods for samples preparation in proteomic research.
A. Bodzoń-Kułakowska (2007)
10.1007/s00253-006-0465-8
Overview of bacterial expression systems for heterologous protein production: from molecular and biochemical fundamentals to commercial systems
K. Terpe (2006)
10.1007/0-306-46826-3_26
Review: novel cysteine proteases of the papain family.
F. Bühling (2000)
10.1016/j.mam.2008.04.003
Protease proteomics: revealing protease in vivo functions using systems biology approaches.
A. Doucet (2008)
10.1021/ac302574f
In-gel nonspecific proteolysis for elucidating glycoproteins: a method for targeted protein-specific glycosylation analysis in complex protein mixtures.
Charles C Nwosu (2013)
10.1002/jssc.201200383
An efficient method for purification of nonspecific lipid transfer protein-1 from rice seeds using kiwifruit actinidin proteolysis and ion exchange chromatography.
Sirous Ghobadi (2012)
10.1016/J.MOLBIOPARA.2007.11.006
Characterization of a PRL protein tyrosine phosphatase from Plasmodium falciparum.
P. R. Pendyala (2008)
10.1002/0471140864.ps0525s71
Overview of Approaches to Preventing and Avoiding Proteolysis During Expression and Purification of Proteins
B. J. Ryan (2013)
10.1126/SCIENCE.277.5332.1602
Blunting Nature's Swiss Army Knife
C. Seife (1997)
10.1016/j.mam.2008.08.001
The ADAM metalloproteinases
D. Edwards (2008)
10.1136/jcp.44.3.236
Measurement of alkaline phosphatase of intestinal origin in plasma by p-bromotetramisole inhibition.
T. Kuwana (1991)
10.1021/jm800765e
Interactions between human glutamate carboxypeptidase II and urea-based inhibitors: structural characterization.
C. Bařinka (2008)
10.1002/1522-2683(200206)23:11<1745::AID-ELPS1745>3.0.CO;2-A
Inhibition of unwanted proteolysis during sample preparation: Evaluation of its efficiency in challenge experiments
L. Castellanos-Serra (2002)
10.1016/j.ab.2012.06.002
Identification and quantification of Fc fusion peptibody degradations by limited proteolysis method.
Lei Yu (2012)
10.1038/nmeth.2371
Zymography methods for visualizing hydrolytic enzymes
Jennifer Vandooren (2013)
10.1007/s12010-013-0096-3
Stabilisation of Recombinant Aequorin by Polyols: Activity, Thermostability and Limited Proteolysis
M. Zeinoddini (2013)
10.1021/pr400442y
Glyco-analytical multispecific proteolysis (Glyco-AMP): a simple method for detailed and quantitative Glycoproteomic characterization.
Serenus Hua (2013)
10.1590/S1517-838246220140359
A biotechnology perspective of fungal proteases
Paula Monteiro de Souza (2015)
10.1002/cmdc.201200057
Activity‐Based Probes for the Study of Proteases: Recent Advances and Developments
Sevnur Serim (2012)
10.1016/j.biotechadv.2011.08.022
Mammalian cell protein expression for biopharmaceutical production.
J. Zhu (2012)
10.1371/journal.pone.0035030
The Threonine Protease Activity of Testes-Specific Protease 50 (TSP50) Is Essential for Its Function in Cell Proliferation
Yuyin Li (2012)
10.1007/978-1-61779-433-9_17
Recombinant protein production in yeasts.
D. Mattanovich (2012)
10.1016/S0092-8674(00)81683-9
The Hallmarks of Cancer
D. Hanahan (2000)
10.1074/jbc.M111.260026
Asparagine Peptide Lyases
N. Rawlings (2011)
10.1142/S0219720011005288
Bioinformatic Approaches for Predicting substrates of Proteases
Jiangning Song (2011)
10.1002/9783527618330
Handbook of Enzyme Inhibitors
H. Zollner (1989)
10.1093/nar/gkp971
MEROPS: the peptidase database
N. Rawlings (2010)
10.1016/S0968-0004(96)10060-8
Molecular mechanisms of the protein serine/threonine phosphatases.
D. Barford (1996)
10.1385/0-89603-126-8:1
Prevention of unwanted proteolysis.
R. Beynon (1988)
10.1042/bj3160777
Demonstration that 1-trans-epoxysuccinyl-L-leucylamido-(4-guanidino) butane (E-64) is one of the most effective low Mr inhibitors of trypsin-catalysed hydrolysis. Characterization by kinetic analysis and by energy minimization and molecular dynamics simulation of the E-64-beta-trypsin complex.
S. Sreedharan (1996)
10.1073/pnas.78.8.4931
The product of the lon (capR) gene in Escherichia coli is the ATP-dependent protease, protease La.
C. Chung (1981)
10.1016/j.biotechadv.2011.09.013
Bacterial expression systems for recombinant protein production: E. coli and beyond.
R. Chen (2012)
10.1016/j.freeradbiomed.2011.08.018
A simple fluorescence labeling method for studies of protein oxidation, protein modification, and proteolysis.
Andrew M Pickering (2012)
10.1016/J.JBIOTEC.2005.04.006
Lon and ClpP proteases participate in the physiological disintegration of bacterial inclusion bodies.
A. Vera (2005)
10.1017/S003118200006176X
Detection of peptidases in Trypanosoma cruzi epimastigotes using chromogenic and fluorogenic substrates.
N. Healy (1992)
10.1074/JBC.274.29.20047
Proteases in Cellular Regulation Minireview Series*
T. Vanaman (1999)
10.1016/0076-6879(91)01043-2
Use of vanadate as protein-phosphotyrosine phosphatase inhibitor.
J. Gordon (1991)
10.1073/pnas.81.6.1619
ATP-dependent degradation of ubiquitin-protein conjugates.
A. Hershko (1984)
10.1021/bi00329a005
Reaction of serine proteases with substituted isocoumarins: discovery of 3,4-dichloroisocoumarin, a new general mechanism based serine protease inhibitor.
J. Harper (1985)
10.1006/abio.1996.0465
Prevention of unwanted proteolysis during extraction of proteins from protease-rich tissue.
M. Hassel (1996)



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