2001
DOI: 10.1006/bbrc.2001.4641
|View full text |Cite
|
Sign up to set email alerts
|

Purification and Structural Analysis of the Hepatitis B Virus PreS1 Expressed from Escherichia coli

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

3
21
0

Year Published

2003
2003
2015
2015

Publication Types

Select...
9

Relationship

1
8

Authors

Journals

citations
Cited by 39 publications
(24 citation statements)
references
References 40 publications
3
21
0
Order By: Relevance
“…1A, lane 3). Similar to the previous study (11), Western blot analysis with anti-preS1 monoclonal antibody indicated a major band of a 39 K protein corresponding to the intact GSTPreS1, several bands of lower molecular weight proteins that most likely represent degradation products of the GST-preS1 fusion protein (Fig. 1B, lane 3).…”
Section: Preparation Of Gst-fusion Construct Of Pres1supporting
confidence: 86%
“…1A, lane 3). Similar to the previous study (11), Western blot analysis with anti-preS1 monoclonal antibody indicated a major band of a 39 K protein corresponding to the intact GSTPreS1, several bands of lower molecular weight proteins that most likely represent degradation products of the GST-preS1 fusion protein (Fig. 1B, lane 3).…”
Section: Preparation Of Gst-fusion Construct Of Pres1supporting
confidence: 86%
“…Such a pattern was observed in other MU type IUPs that contain more than one pre-structured motifs (4,29). Typically, the population of transient pre-structured motifs in a mostly unstructured type of IUPs is less than 20% (4,31). In p53 TAD where the population of transient motifs is ∼10%, the CD spectral change at 220 nm caused by destruction of pre-structured motifs due to addition of denaturants could be clearly measured (28).…”
Section: The Overall Structural State Of Vp16 Tadmentioning
confidence: 81%
“…The concentrationdependent increase of RU signals clearly confirms that there are specific interactions between the Fab and all the epitope-near preS1 regions. The interactions of these four preS1 peptides for the Fab were weak with the equilibrium dissociation constant (K d ) values of 1-2 mM range: 1.54, 1.63, 2.04, and 1.99 mM for preS1 (1-11), preS1 (27)(28)(29)(30)(31)(32)(33)(34)(35), preS1 (66-76), and preS1 (95-104), respectively. Although this binding affinity seems low, it is comparable to the affinities observed for germline antibody binding [28] and TCR-peptide/MHC (pMHC) interactions [35].…”
Section: Resultsmentioning
confidence: 99%
“…HzKR127 Fab in 25 mM sodium acetate, pH 5.5 was immobilized to a channel of CM5 sensor chip using an amine coupling kit (BIAcore AB) and the control flow-subtracted sensograms are obtained. The peptide concentrations range from 10 to 640 nM for preS1 (36-46), from 5 to 80 nM for preS1 (1-119), and from 100 to 800 lM for preS1 (1-11), preS1 (27)(28)(29)(30)(31)(32)(33)(34)(35), preS1 (66-76), and preS1 (95-104). Kinetic measurements were made and kinetic constants were derived with the BIAevaluation Version 3.0 software (BIAcore AB).…”
Section: Surface Plasma Resonance Experimentsmentioning
confidence: 99%