New Role for an Old Probe:  Affinity Labeling of Oxylipid Protein Conjugates byN‘-Aminooxymethylcarbonylhydrazinod-biotin

2006 ◽  
Vol 78 (19) ◽  
pp. 6847-6854 ◽  
Author(s):  
Juan Chavez ◽  
Jianyong Wu ◽  
Bingnan Han ◽  
Woon-Gye Chung ◽  
Claudia S. Maier
Keyword(s):  
Affinity Labeling ◽  
Protein Conjugates ◽  
Probe Affinity

m-[o-(2-Chloro-5-Fluorosulfonylphenylureido)Phenoxybutoxy]Benzamidine: Affinity Labeling Reagent Which Can Identify Secondary Binding Sites of Coagulation Complement and Fibrinolytic Serine Proteases

1979 ◽  
Author(s):  
D Bing ◽  
D Robison ◽  
J Andrews ◽  
R Laura
Keyword(s):  
Binding Sites ◽  
Serine Proteases ◽  
Enzyme Inhibitor ◽  
Molecular Model ◽  
Factor Xa ◽  
Affinity Labeling ◽  
Catalytic Center ◽  
Inhibitor Complex ◽  
Polypeptide Chains ◽  
Kinetics Of

We have determined that m-[o-(2-chloro-5-fluorosulfonylphenylureido)phenoxybutoxy]benza-midine [mCP(PBA)-F] is an affinity labeling reagent which labels both polypeptide chains of thrombin, factor Xa, complement component CIS and plasmin. As this means it is reacting outside of the catalytic center, we have called this reagent an exo-site affinity labeling reagent. Progressive irreversible inhibition of these enzymes by this reagent is rapid (k1st 2.5-4.6 x 10-3sec-1), the kinetics of inactivation are consistent with inhibition proceding via formation of a specific enzyme-inhibitor complex analogous to a Michaelis-Menton complex (KL - 115-26 μM), and diisopropylfluorophosphate or p-amidino-phenylmethanesulfonyfluoride Prevent labeling by [3H]mCP(PBA)-F. A molecular model of mCP(PBA)-F shows that the reactive SO2F group can be 17 A from the cationic amidine. The data are consistent with the hypothesis that both peptide chains are required for the specific proteolytic activity exhibited by these proteases and that the peptide chain which does not contain the active site serine is close to the catalytic center. (Supported by NIH and AHA grants

Cardiological Biopharmaceuticals in the Conception of Drug Targeting Delivery: Practical Results and Research Perspectives

Acta Naturae ◽  
2012 ◽  
Vol 4 (3) ◽  
pp. 72-81 ◽  
Author(s):  
A. V. Maksimenko
Keyword(s):  
Cell Adhesion Molecules ◽  
Drug Targeting ◽  
Interventional Procedures ◽  
Target Localization ◽  
Clinical Use ◽  
Protein Conjugates ◽  
Research Perspectives ◽  
Significant Interest ◽  
Targeting Delivery ◽  
Molecular Sizes

The results of the clinical use of thrombolytic and antithrombotic preparations developed on the basis of protein conjugates obtained within the framework of the conception of drug targeting delivery in the organism are considered. A decrease has been noted in the number of biomedical projects focused on these derivatives as a result of various factors: the significant depletion of financial and organizational funds, the saturation of the pharmaceutical market with preparations of this kind, and the appearance of original means for interventional procedures. Factors that actively facilitate the conspicuous potentiation of the efficacy of bioconjugates were revealed: the biomedical testing of protein domains and their selected combinations, the optimization of molecular sizes for the bioconjugates obtained, the density of target localization, the application of cell adhesion molecules as targets, and the application of connected enzyme activities. Enzyme antioxidants and the opportunity for further elaboration of the drug delivery conception via the elucidation and formation of therapeutic targets for effective drug reactions by means of pharmacological pre- and postconditioning of myocardium arouse significant interest.

PRODUCTION AND CHARACTERIZATION OF ANTIBODIES ELICITED BY DIFFERENT ALDOSTERONE-PROTEIN CONJUGATES

1972 ◽  
Vol 68 (3_Suppl) ◽  
pp. S32
Author(s):  
W. Vetter ◽  
E. Freedlender ◽  
E. Haber
Keyword(s):  
Protein Conjugates

Preparation of conjugates of uridine with proteins by the imido ester condensation method

1981 ◽  
Vol 46 (4) ◽  
pp. 933-940 ◽  
Author(s):  
Helmut Pischel ◽  
Antonín Holý ◽  
Günther Wagner
Keyword(s):  
Human Serum ◽  
Acid Hydrolysis ◽  
Ester Hydrochloride ◽  
Protein Conjugates ◽  
Condensation Method ◽  
Ester Condensation ◽  
Acid Catalyzed

Reaction of 5'-O-p-toluenesulfonyl-2',3'-O-isopropylideneuridine (I) with sodium 4-cyanophenoxide afforded 2',3'-O-isopropylidene-5'-O-(4-cyanophenyl)uridine (II) which was converted by acid hydrolysis into 5'-O-(4-cyanophenyl)uridine (IIIa). Acid-catalyzed addition of ethanol to compound IIIa gave the imido ester hydrochloride IIIb which on reaction with ammonia or ethylamine was transformed into the amidine derivatives IIIc and IIId. Compound IIIb reacted with human serum albumine or bovine gamma-globuline at pH 9.2 to give protein conjugates with uridine, bound covalently by an amidine bond (IIIe,f).

scholarly journals Identification of a nerve growth factor receptor protein in sympathetic ganglia membranes by affinity labeling.

1981 ◽  
Vol 256 (18) ◽  
pp. 9419-9424 ◽  
Author(s):  
J. Massague ◽  
B.J. Guillette ◽  
M.P. Czech ◽  
C.J. Morgan ◽  
R.A. Bradshaw
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Growth Factor Receptor ◽  
Sympathetic Ganglia ◽  
Nerve Growth Factor Receptor ◽  
Receptor Protein ◽  
Affinity Labeling ◽  
Nerve Growth

scholarly journals The ATP binding site on rho protein. Affinity labeling of Lys181 by pyridoxal 5′-diphospho-5′-adenosine.

1988 ◽  
Vol 263 (35) ◽  
pp. 18810-18815 ◽  
Author(s):  
A J Dombroski ◽  
J R LaDine ◽  
R L Cross ◽  
T Platt
Keyword(s):  
Binding Site ◽  
Affinity Labeling ◽  
Atp Binding ◽  
Atp Binding Site ◽  
Protein Affinity ◽  
Rho Protein

scholarly journals Selective affinity labeling and molecular characterization of hepatic alpha 1-adrenergic receptors with [3H]phenoxybenzamine.

1983 ◽  
Vol 258 (1) ◽  
pp. 326-332 ◽  
Author(s):  
G Kunos ◽  
W H Kan ◽  
R Greguski ◽  
J C Venter
Keyword(s):  
Molecular Characterization ◽  
Adrenergic Receptors ◽  
Affinity Labeling
Sign in / Sign up

Export Citation Format

Share Document