A styryl based fluorogenic probe with high affinity for a cyclodextrin derivative

2019 ◽  
Vol 17 (28) ◽  
pp. 6895-6904 ◽  
Author(s):  
Goutam Chakraborty ◽  
Alok K. Ray ◽  
Prabhat K. Singh ◽  
Haridas Pal
Keyword(s):  
Temperature Sensor ◽  
Association Constant ◽  
Biological Marker ◽  
High Association ◽  
High Affinity ◽  
Cyclodextrin Derivative ◽  
Near Ir ◽  
Fluorogenic Probe ◽  
Very High

A styryl-based fluorogenic near-IR probe registers a very high association constant with sulfobutylether substituted β-cyclodextrin host, having prospects as biological marker and improved pH and temperature sensor.

Effects of Heparin Oligosaccharides with High Affinity for Antithrombin III in Experimental Venous Thrombosis

1982 ◽  
Vol 47 (03) ◽  
pp. 244-248 ◽  
Author(s):  
D P Thomas ◽  
Rosemary E Merton ◽  
T W Barrowcliffe ◽  
L Thunberg ◽  
U Lindahl
Keyword(s):  
Antithrombin Iii ◽  
Specific Activity ◽  
High Specific Activity ◽  
Factor Xa ◽  
Blood Levels ◽  
Thrombin Time ◽  
High Affinity ◽  
Very High

SummaryThe in vitro and in vivo characteristics of two oligosaccharide heparin fragments have been compared to those of unfractionated mucosal heparin. A decasaccharide fragment had essentially no activity by APTT or calcium thrombin time assays in vitro, but possessed very high specific activity by anti-Factor Xa assays. When injected into rabbits at doses of up to 80 ¼g/kg, this fragment was relatively ineffective in impairing stasis thrombosis despite producing high blood levels by anti-Xa assays. A 16-18 monosaccharide fragment had even higher specific activity (almost 2000 iu/mg) by chromogenic substrate anti-Xa assay, with minimal activity by APTT. When injected in vivo, this fragment gave low blood levels by APTT, very high anti-Xa levels, and was more effective in preventing thrombosis than the decasaccharide fragment. However, in comparison with unfractionated heparin, the 16-18 monosaccharide fragment was only partially effective in preventing thrombosis, despite producing much higher blood levels by anti-Xa assays.It is concluded that the high-affinity binding of a heparin fragment to antithrombin III does not by itself impair venous thrombogenesis, and that the anti-Factor Xa activity of heparin is only a partial expression of its therapeutic potential.

scholarly journals Tityus serrulatus venom contains two classes of toxins. Tityus gamma toxin is a new tool with a very high affinity for studying the Na+ channel.

1982 ◽  
Vol 257 (21) ◽  
pp. 12553-12558
Author(s):  
J Barhanin ◽  
J R Giglio ◽  
P Léopold ◽  
A Schmid ◽  
S V Sampaio ◽  
...  
Keyword(s):  
Na Channel ◽  
High Affinity ◽  
Tityus Serrulatus ◽  
Tityus Serrulatus Venom ◽  
Very High

N-terminal fragment of the anti-angiogenic human endostatin binds copper(II) with very high affinity

2009 ◽  
Vol 103 (7) ◽  
pp. 940-947 ◽  
Author(s):  
András Kolozsi ◽  
Attila Jancsó ◽  
Nóra V. Nagy ◽  
Tamás Gajda
Keyword(s):  
High Affinity ◽  
Terminal Fragment ◽  
Very High

scholarly journals The effect of temperature on the oxygen dissociation curves of whole blood of larval and adult lampreys (Geotria australis)

1982 ◽  
Vol 97 (1) ◽  
pp. 253-261
Author(s):  
D. J. Macey ◽  
I. C. Potter
Keyword(s):  
Whole Blood ◽  
Life Cycle Stage ◽  
Effect Of Temperature ◽  
High Affinity ◽  
Oxygen Dissociation ◽  
Geotria Australis ◽  
Oxygen Tensions ◽  
Dissociation Curves ◽  
Hill Plots ◽  
Very High

1. Oxygen dissociation curves of the whole blood of larvae and adults of the Southern Hemisphere lamprey Geotria australis have been determined between pH 6.8 and 8.2 at 5, 15 and 25 degrees C. 2. The P50's at temperatures of 5, 15 and 25 degrees C and a pH of 7.75 were respectively 0.57, 0.92 and 1.19 mmHg in larvae and 6.9, 10.3 and 19.0 mmHg in adults. 3. The relatively very high affinity of larval blood for oxygen may reflect an adaptation to low environmental oxygen tensions. 4. The Bohr shift was not significantly affected by either temperature or life-cycle stage. 5. The slope (n) in Hill plots increased with temperature and oxygen saturation, and was greater in adults than in larvae.

scholarly journals Degradation of Chlorobenzenes at Nanomolar Concentrations byBurkholderia sp. Strain PS14 in Liquid Cultures and in Soil

1999 ◽  
Vol 65 (6) ◽  
pp. 2547-2552 ◽  
Author(s):  
Peter Rapp ◽  
Kenneth N. Timmis
Keyword(s):  
Incubation Period ◽  
Detection Limits ◽  
Batch Experiments ◽  
Sorptive Capacity ◽  
Residual Concentration ◽  
Soil Microcosms ◽  
Initial Concentration ◽  
High Affinity ◽  
Low Cell Density ◽  
Very High

ABSTRACT The utilization of 1,2,4,5-tetrachloro-, 1,2,4-trichloro-, the three isomeric dichlorobenzenes and fructose as the sole carbon and energy sources at nanomolar concentrations was studied in batch experiments with Burkholderia sp. strain PS14. In liquid culture, all chlorobenzenes were metabolized within 1 h from their initial concentration of 500 nM to below their detection limits of 0.5 nM for 1,2,4,5-tetrachloro- and 1,2,4-trichlorobenzene and 7.5 nM for the three dichlorobenzene isomers, with 63% mineralization of the tetra- and trichloroisomers. Fructose at the same initial concentration was, in contrast, metabolized over a 4-h incubation period down to a residual concentration of approximately 125 nM with 38% mineralization during this time. In soil microcosms, Burkholderia sp. strain PS14 metabolized tetrachlorobenzene present at 64.8 ppb and trichlorobenzene present at 54.4 ppb over a 72-h incubation period to below the detection limits of 0.108 and 0.09 ppb, respectively, with approximately 80% mineralization. A high sorptive capacity ofBurkholderia sp. strain PS14 for 1,2,4,5-tetrachlorobenzene was found at very low cell density. The results demonstrate thatBurkholderia sp. strain PS14 exhibits a very high affinity for chlorobenzenes at nanomolar concentrations.

SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange

1993 ◽  
Vol 13 (3) ◽  
pp. 1449-1455
Author(s):  
S Felder ◽  
M Zhou ◽  
P Hu ◽  
J Ureña ◽  
A Ullrich ◽  
...  
Keyword(s):  
Growth Factor ◽  
Intracellular Signaling ◽  
Interaction Analysis ◽  
Growth Factor Receptors ◽  
Signaling Molecules ◽  
Sequence Motif ◽  
Sh2 Domains ◽  
High Affinity ◽  
Phosphorylated Peptides ◽  
Very High

src homology 2 (SH2) domains of intracellular signaling molecules such as phospholipase C-gamma and phosphatidylinositol 3'-kinase-associated protein p85 represent recognition motifs for specific phosphotyrosine-containing regions on activated growth factor receptors. The binding of SH2 domains to activated growth factor receptors controls the interaction with signaling molecules and the regulation of their activities. In this report, we describe the kinetic parameters and binding affinities of SH2 domains of p85 toward short phosphotyrosine-containing peptides with the amino acid sequence motif YMXM, derived from a major insulin receptor substrate, IRS-1, by using real time biospecific interaction analysis (BIAcore). Associations were specific and of very high affinity, with dissociation constants of 0.3 to 3 nM, between phosphopeptides and the two separate SH2 domains contained within p85. Nonphosphorylated peptides showed no measurable binding, and the interactions were specific for the primary sequence very close to the phosphotyrosine residue. Moreover, the interactions between phosphopeptides and SH2 domains of other signaling molecules were of much lower affinity. Interestingly, the binding of the SH2 domains to the tyrosine-phosphorylated peptides was of high affinity as a result of a very high on rate, of 3 x 10(7) to 40 x 10(7)/M/s; at the same time, the rate of dissociation, of 0.11 to 0.19/s, was rapid, allowing for rapid exchange of associating proteins with the tyrosine phosphorylation sites.

scholarly journals SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange.

1993 ◽  
Vol 13 (3) ◽  
pp. 1449-1455 ◽  
Author(s):  
S Felder ◽  
M Zhou ◽  
P Hu ◽  
J Ureña ◽  
A Ullrich ◽  
...  
Keyword(s):  
Growth Factor ◽  
Intracellular Signaling ◽  
Interaction Analysis ◽  
Growth Factor Receptors ◽  
Signaling Molecules ◽  
Sequence Motif ◽  
Sh2 Domains ◽  
High Affinity ◽  
Phosphorylated Peptides ◽  
Very High

src homology 2 (SH2) domains of intracellular signaling molecules such as phospholipase C-gamma and phosphatidylinositol 3'-kinase-associated protein p85 represent recognition motifs for specific phosphotyrosine-containing regions on activated growth factor receptors. The binding of SH2 domains to activated growth factor receptors controls the interaction with signaling molecules and the regulation of their activities. In this report, we describe the kinetic parameters and binding affinities of SH2 domains of p85 toward short phosphotyrosine-containing peptides with the amino acid sequence motif YMXM, derived from a major insulin receptor substrate, IRS-1, by using real time biospecific interaction analysis (BIAcore). Associations were specific and of very high affinity, with dissociation constants of 0.3 to 3 nM, between phosphopeptides and the two separate SH2 domains contained within p85. Nonphosphorylated peptides showed no measurable binding, and the interactions were specific for the primary sequence very close to the phosphotyrosine residue. Moreover, the interactions between phosphopeptides and SH2 domains of other signaling molecules were of much lower affinity. Interestingly, the binding of the SH2 domains to the tyrosine-phosphorylated peptides was of high affinity as a result of a very high on rate, of 3 x 10(7) to 40 x 10(7)/M/s; at the same time, the rate of dissociation, of 0.11 to 0.19/s, was rapid, allowing for rapid exchange of associating proteins with the tyrosine phosphorylation sites.

scholarly journals A single domain of yeast poly(A)-binding protein is necessary and sufficient for RNA binding and cell viability.

1987 ◽  
Vol 7 (9) ◽  
pp. 3268-3276 ◽  
Author(s):  
A B Sachs ◽  
R W Davis ◽  
R D Kornberg
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Association Constant ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Binding Protein ◽  
High Affinity ◽  
Terminal Domain ◽  
Necessary And Sufficient

The poly(A)-binding protein (PAB) gene of Saccharomyces cerevisiae is essential for cell growth. A 66-amino acid polypeptide containing half of a repeated N-terminal domain can replace the entire protein in vivo. Neither an octapeptide sequence conserved among eucaryotic RNA-binding proteins nor the C-terminal domain of PAB is required for function in vivo. A single N-terminal domain is nearly identical to the entire protein in the number of high-affinity sites for poly(A) binding in vitro (one site with an association constant of approximately 2 X 10(7) M-1) and in the size of the binding site (12 A residues). Multiple N-terminal domains afford a mechanism of PAB transfer between poly(A) strands.

Evaluation of a new free-thyroxin assay.

1981 ◽  
Vol 27 (12) ◽  
pp. 2022-2024 ◽  
Author(s):  
M L Wellby ◽  
L Guthrie ◽  
C P Reilly
Keyword(s):  
Oral Contraceptives ◽  
Reference Interval ◽  
Free T4 ◽  
Single Tube ◽  
High Affinity ◽  
Assay Precision ◽  
Very High ◽  
Interassay Precision ◽  
Better Than

Abstract The Amerlex Free Thyroxin (T4) Radioimmunoassay Kit (Amersham International Ltd.) is a new direct equilibrium radioimmunoassay for free T4 based on an antiserum with very high affinity for T4, and a unique 125I-labeled T4 analog as tracer. It is a very simple single-tube radioimmunoassay, making use of Amerlex particles to separate antibody-bound from free species. Interassay precision (CV) is 3.7% at 13 pmol/L and 2.3% at 30 pmol/L; within-assay precision is 4.2% at 21 pmol/L. The reference interval is 11-22 pmol/L. The assay did not misclassify any patients tested who had untreated myxedema or untreated thyrotoxicosis. The free T4 assay excelled both the free T4 index and the T4/T4-binding globulin ratio in correcting for increased thyroxin-binding globulin from pregnancy, and it was better than the index but not better than the ratio in correcting for increased thyroxin-binding globulin in users of oral contraceptives.

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