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Activity of the Human Rhinovirus 3C Protease Studied in Various Buffers, Additives and Detergents Solutions for Recombinant Protein Production

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Standard

Activity of the Human Rhinovirus 3C Protease Studied in Various Buffers, Additives and Detergents Solutions for Recombinant Protein Production. / Ullah, Raheem; Shah, Majid Ali; Tufail, Soban; Ismat, Fouzia; Imran, Muhammad; Iqbal, Mazhar; Mirza, Osman; Rhaman, Moazur.

I: PloS one, Bind 11, Nr. 4, e0153436, 2016.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Ullah, R, Shah, MA, Tufail, S, Ismat, F, Imran, M, Iqbal, M, Mirza, O & Rhaman, M 2016, 'Activity of the Human Rhinovirus 3C Protease Studied in Various Buffers, Additives and Detergents Solutions for Recombinant Protein Production', PloS one, bind 11, nr. 4, e0153436. https://doi.org/10.1371/journal.pone.0153436

APA

Ullah, R., Shah, M. A., Tufail, S., Ismat, F., Imran, M., Iqbal, M., ... Rhaman, M. (2016). Activity of the Human Rhinovirus 3C Protease Studied in Various Buffers, Additives and Detergents Solutions for Recombinant Protein Production. PloS one, 11(4), [e0153436]. https://doi.org/10.1371/journal.pone.0153436

Vancouver

Ullah R, Shah MA, Tufail S, Ismat F, Imran M, Iqbal M o.a. Activity of the Human Rhinovirus 3C Protease Studied in Various Buffers, Additives and Detergents Solutions for Recombinant Protein Production. PloS one. 2016;11(4). e0153436. https://doi.org/10.1371/journal.pone.0153436

Author

Ullah, Raheem ; Shah, Majid Ali ; Tufail, Soban ; Ismat, Fouzia ; Imran, Muhammad ; Iqbal, Mazhar ; Mirza, Osman ; Rhaman, Moazur. / Activity of the Human Rhinovirus 3C Protease Studied in Various Buffers, Additives and Detergents Solutions for Recombinant Protein Production. I: PloS one. 2016 ; Bind 11, Nr. 4.

Bibtex

@article{50444e49ca8e47cb89f7b54d0e5765ca,
title = "Activity of the Human Rhinovirus 3C Protease Studied in Various Buffers, Additives and Detergents Solutions for Recombinant Protein Production",
abstract = "Proteases are widely used to remove affinity and solubility tags from recombinant proteins to avoid potential interference of these tags with the structure and function of the fusion partner. In recent years, great interest has been seen in use of the human rhinovirus 3C protease owing to its stringent sequence specificity and enhanced activity. Like other proteases, activity of the human rhinovirus 3C protease can be affected in part by the buffer components and additives that are generally employed for purification and stabilization of proteins, hence, necessitate their removal by tedious and time-consuming procedures before proteolysis can occur. To address this issue, we examined the effect of elution buffers used for common affinity based purifications, salt ions, stability/solubility and reducing agents, and detergents on the activity of the human rhinovirus 3C protease using three different fusion proteins at 4°C, a temperature of choice for purification of many proteins. The results show that the human rhinovirus 3C protease performs better at 4°C than the frequently used tobacco etch virus protease and its activity was insensitive to most of the experimental conditions tested. Though number of fusion proteins tested is limited, we expect that these finding will facilitate the use of the human rhinovirus 3C protease in recombinant protein production for pharmaceutical and biotechnological applications.",
author = "Raheem Ullah and Shah, {Majid Ali} and Soban Tufail and Fouzia Ismat and Muhammad Imran and Mazhar Iqbal and Osman Mirza and Moazur Rhaman",
year = "2016",
doi = "10.1371/journal.pone.0153436",
language = "English",
volume = "11",
journal = "P L o S One",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "4",

}

RIS

TY - JOUR

T1 - Activity of the Human Rhinovirus 3C Protease Studied in Various Buffers, Additives and Detergents Solutions for Recombinant Protein Production

AU - Ullah, Raheem

AU - Shah, Majid Ali

AU - Tufail, Soban

AU - Ismat, Fouzia

AU - Imran, Muhammad

AU - Iqbal, Mazhar

AU - Mirza, Osman

AU - Rhaman, Moazur

PY - 2016

Y1 - 2016

N2 - Proteases are widely used to remove affinity and solubility tags from recombinant proteins to avoid potential interference of these tags with the structure and function of the fusion partner. In recent years, great interest has been seen in use of the human rhinovirus 3C protease owing to its stringent sequence specificity and enhanced activity. Like other proteases, activity of the human rhinovirus 3C protease can be affected in part by the buffer components and additives that are generally employed for purification and stabilization of proteins, hence, necessitate their removal by tedious and time-consuming procedures before proteolysis can occur. To address this issue, we examined the effect of elution buffers used for common affinity based purifications, salt ions, stability/solubility and reducing agents, and detergents on the activity of the human rhinovirus 3C protease using three different fusion proteins at 4°C, a temperature of choice for purification of many proteins. The results show that the human rhinovirus 3C protease performs better at 4°C than the frequently used tobacco etch virus protease and its activity was insensitive to most of the experimental conditions tested. Though number of fusion proteins tested is limited, we expect that these finding will facilitate the use of the human rhinovirus 3C protease in recombinant protein production for pharmaceutical and biotechnological applications.

AB - Proteases are widely used to remove affinity and solubility tags from recombinant proteins to avoid potential interference of these tags with the structure and function of the fusion partner. In recent years, great interest has been seen in use of the human rhinovirus 3C protease owing to its stringent sequence specificity and enhanced activity. Like other proteases, activity of the human rhinovirus 3C protease can be affected in part by the buffer components and additives that are generally employed for purification and stabilization of proteins, hence, necessitate their removal by tedious and time-consuming procedures before proteolysis can occur. To address this issue, we examined the effect of elution buffers used for common affinity based purifications, salt ions, stability/solubility and reducing agents, and detergents on the activity of the human rhinovirus 3C protease using three different fusion proteins at 4°C, a temperature of choice for purification of many proteins. The results show that the human rhinovirus 3C protease performs better at 4°C than the frequently used tobacco etch virus protease and its activity was insensitive to most of the experimental conditions tested. Though number of fusion proteins tested is limited, we expect that these finding will facilitate the use of the human rhinovirus 3C protease in recombinant protein production for pharmaceutical and biotechnological applications.

U2 - 10.1371/journal.pone.0153436

DO - 10.1371/journal.pone.0153436

M3 - Journal article

C2 - 27093053

VL - 11

JO - P L o S One

JF - P L o S One

SN - 1932-6203

IS - 4

M1 - e0153436

ER -

ID: 160985737