Asset Details
MbrlCatalogueTitleDetail
Do you wish to reserve the book?
Application of Ni(II)-Assisted Peptide Bond Hydrolysis to Non-Enzymatic Affinity Tag Removal
by
Kopera, Edyta
, Belczyk-Ciesielska, Agnieszka
, Bal, Wojciech
in
Affinity
/ Affinity Labels - chemistry
/ Affinity Labels - isolation & purification
/ Amino Acid Motifs
/ Biochemistry
/ Biological activity
/ Biology
/ Biophysics
/ Carcinogens
/ Chemistry
/ Cleavage
/ Detergents
/ Dithiothreitol
/ Engineering
/ Enzymes
/ Fusion protein
/ Humans
/ Hydrolysis
/ Hydroxylamine - chemistry
/ Libraries
/ Nickel
/ Nickel - chemistry
/ Oligopeptides - chemistry
/ Peptides
/ pH effects
/ Proteins
/ Proteolysis
/ Solutions
/ Substrate Specificity
/ Transcription factors
/ Ubiquitin - chemistry
2012
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
You are currently in the queue to collect this book. You will be notified once it is your turn to collect the book.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Application of Ni(II)-Assisted Peptide Bond Hydrolysis to Non-Enzymatic Affinity Tag Removal
by
Kopera, Edyta
, Belczyk-Ciesielska, Agnieszka
, Bal, Wojciech
in
Affinity
/ Affinity Labels - chemistry
/ Affinity Labels - isolation & purification
/ Amino Acid Motifs
/ Biochemistry
/ Biological activity
/ Biology
/ Biophysics
/ Carcinogens
/ Chemistry
/ Cleavage
/ Detergents
/ Dithiothreitol
/ Engineering
/ Enzymes
/ Fusion protein
/ Humans
/ Hydrolysis
/ Hydroxylamine - chemistry
/ Libraries
/ Nickel
/ Nickel - chemistry
/ Oligopeptides - chemistry
/ Peptides
/ pH effects
/ Proteins
/ Proteolysis
/ Solutions
/ Substrate Specificity
/ Transcription factors
/ Ubiquitin - chemistry
2012
Oops! Something went wrong.
While trying to remove the title from your shelf something went wrong :( Kindly try again later!
Do you wish to request the book?
Application of Ni(II)-Assisted Peptide Bond Hydrolysis to Non-Enzymatic Affinity Tag Removal
by
Kopera, Edyta
, Belczyk-Ciesielska, Agnieszka
, Bal, Wojciech
in
Affinity
/ Affinity Labels - chemistry
/ Affinity Labels - isolation & purification
/ Amino Acid Motifs
/ Biochemistry
/ Biological activity
/ Biology
/ Biophysics
/ Carcinogens
/ Chemistry
/ Cleavage
/ Detergents
/ Dithiothreitol
/ Engineering
/ Enzymes
/ Fusion protein
/ Humans
/ Hydrolysis
/ Hydroxylamine - chemistry
/ Libraries
/ Nickel
/ Nickel - chemistry
/ Oligopeptides - chemistry
/ Peptides
/ pH effects
/ Proteins
/ Proteolysis
/ Solutions
/ Substrate Specificity
/ Transcription factors
/ Ubiquitin - chemistry
2012
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Application of Ni(II)-Assisted Peptide Bond Hydrolysis to Non-Enzymatic Affinity Tag Removal
Journal Article
Application of Ni(II)-Assisted Peptide Bond Hydrolysis to Non-Enzymatic Affinity Tag Removal
2012
Request Book From Autostore
and Choose the Collection Method
Overview
In this study, we demonstrate a non-enzymatic method for hydrolytic peptide bond cleavage, applied to the removal of an affinity tag from a recombinant fusion protein, SPI2-SRHWAP-His(6). This method is based on a highly specific Ni(II) reaction with (S/T)XHZ peptide sequences. It can be applied for the protein attached to an affinity column or to the unbound protein in solution. We studied the effect of pH, temperature and Ni(II) concentration on the efficacy of cleavage and developed an analytical protocol, which provides active protein with a 90% yield and ∼100% purity. The method works well in the presence of non-ionic detergents, DTT and GuHCl, therefore providing a viable alternative for currently used techniques.
This website uses cookies to ensure you get the best experience on our website.