scholarly journals Probes for Photoaffinity Labelling of Kinases

ChemBioChem ◽  
2021 ◽  
Author(s):  
Dimitris Korovesis ◽  
Hester A. Beard ◽  
Christel Mérillat ◽  
Steven H. L. Verhelst
Keyword(s):  
Photoaffinity Labelling

Photoreaction of N-butyl 3,4-dimethoxy-6-nitrobenzamide with butylamine. A model study for lysine-directed photoaffinity labelling

1987 ◽  
Vol 52 (7) ◽  
pp. 1780-1785 ◽  
Author(s):  
Petr Kuzmič ◽  
Libuše Pavlíčková ◽  
Milan Souček
Keyword(s):  
Nitro Group ◽  
Aromatic Ring ◽  
Ultraviolet Irradiation ◽  
Title Compound ◽  
Reductive Coupling ◽  
Photoaffinity Labelling ◽  
Photolysis Rate ◽  
Model Study ◽  
A Minor

Ultraviolet irradiation of the title compound I in the presence of butylamine gave predominantly products of nucleophilic photosubstitution by the amine, i.e., nitroanilines IIa and IIb. Besides, small amounts of products of hydrolysis (phenol III) and reductive coupling (azoxybenzene IV) were also formed. Comparison of the overall photolysis rate of I with that of 3,4-dimethoxy-1-nitrobenzene (V) indicates a minor loss of reactivity, most probably due to some deviation from coplanarity of the activating nitro group and the aromatic ring.

scholarly journals A photoaffinity labelling study of the messenger RNA-binding region of Escherichia coli ribosomes

1978 ◽  
Vol 5 (9) ◽  
pp. 3389-3408 ◽  
Author(s):  
Harry Towbin ◽  
David Elson
Keyword(s):  
Escherichia Coli ◽  
Messenger Rna ◽  
Rna Binding ◽  
Binding Region ◽  
Photoaffinity Labelling

Nucleotides part XXX Chemical synthesis of adenylyl-(2? ? 5?)-adenylyl-(2? ? 5?)-8-azidoadenosine, and activation and photoaffinity labelling of RNase L by [32P]p5?A2?p5?A2?p5?N38A

1989 ◽  
Vol 72 (6) ◽  
pp. 1354-1361 ◽  
Author(s):  
Ramamurthy Charubala ◽  
Wolfgang Pfleiderer ◽  
Robert W. Sobol ◽  
Shi Wu Li ◽  
Robert J. Suhadolnik
Keyword(s):  
Chemical Synthesis ◽  
Rnase L ◽  
Photoaffinity Labelling

Yeast Phenylalanyl-tRNA Synthetase. Affinity and Photoaffinity Labelling of the Stereospecific Binding Sites

1979 ◽  
Vol 97 (2) ◽  
pp. 481-494 ◽  
Author(s):  
Mireille BALTZINGER ◽  
Franco FASIOLO ◽  
Pierre REMY
Keyword(s):  
Binding Sites ◽  
Trna Synthetase ◽  
Photoaffinity Labelling

The nucleophilic aromatic photosubstitution in photoaffinity labelling. A model study of a cycloheximide derivative.

1985 ◽  
Vol 26 (20) ◽  
pp. 2489-2492 ◽  
Author(s):  
A. Castelló ◽  
J. Marquet ◽  
M. Moreno-Mañas ◽  
X. Sirera
Keyword(s):  
Photoaffinity Labelling ◽  
Model Study

scholarly journals Photoaffinity labelling of human poly(ADP-ribose) polymerase catalytic domain

1997 ◽  
Vol 322 (2) ◽  
pp. 469-475 ◽  
Author(s):  
Hyuntae KIM ◽  
Myron K. JACOBSON ◽  
Véronique ROLLI ◽  
Josiane MÉNISSIER-de MURCIA ◽  
Joseph REINBOLT ◽  
...  
Keyword(s):  
Catalytic Domain ◽  
Insertion Site ◽  
Site Directed Mutagenesis ◽  
Crystallographic Structure ◽  
Reverse Phase Hplc ◽  
Reverse Phase ◽  
Photoaffinity Labelling ◽  
Adenine Ring ◽  
Boronate Affinity Chromatography ◽  
Binding Residues

Photoaffinity labelling of the human poly(ADP-ribose) polymerase (PARP) catalytic domain (40 kDa) with the NAD+ photoaffinity analogue 2-azido-[α-32P]NAD+ has been used to identify NAD+-binding residues. In the presence of UV, photoinsertion of the analogue was observed with a stoichiometry of 0.73 mol of 2-azido-[α-32P]NAD+ per mol of catalytic domain. Competition experiments indicated that 3-aminobenzamide strongly protected the insertion site. Residues binding the adenine ring of NAD+ were identified by trypsin digestion and boronate affinity chromatography in combination with reverse-phase HPLC. Two major NAD+-binding residues, Trp1014 of peptide Thr1011–Trp1014 and Lys893 of peptide Ile879 –Lys893, were identified. The site-directed mutagenesis of these two residues revealed that Lys893, but not Trp1014, is critical for activity. The close positioning of Lys893 near the adenine ring of NAD+ has been confirmed by the recently solved crystallographic structure of the chicken PARP catalytic domain [Ruf, Ménissier-de Murcia, de Murcia and Schulz (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 7481–7485].

scholarly journals Photoaffinity labelling of cyclic GMP-binding proteins in human platelets

1993 ◽  
Vol 294 (2) ◽  
pp. 329-333 ◽  
Author(s):  
K M Tang ◽  
J L Sherwood ◽  
R J Haslam
Keyword(s):  
Protein Kinase ◽  
Cyclic Gmp ◽  
Binding Proteins ◽  
Protein S ◽  
Human Platelets ◽  
Dependent Protein Kinase ◽  
Camp Phosphodiesterase ◽  
Proteolytic Fragment ◽  
Photoaffinity Labelling ◽  
Dependent Protein

The photoaffinity labelling of platelet cyclic GMP (cGMP)-binding proteins by [32P]cGMP was studied; at least five labelled proteins (110, 80, 55, 49 and 38 kDa) were detected in platelet cytosol and four (80, 65, 49 and 38 kDa) in platelet membranes. The 110 kDa species was identified as cGMP-inhibited cyclic AMP (cAMP) phosphodiesterase (PDE III) by immunoprecipitation and by the inhibition of photolabelling by specific inhibitors of this enzyme. Similarly, the 80 kDa species was identified as cGMP-dependent protein kinase by immunoprecipitation and by the effects of cGMP analogues on photolabelling. Addition of cAMP greatly enhanced the labelling of this 80 kDa protein, implying the existence of a potentially important interaction between the effects of cGMP and cAMP. The 65 kDa photolabelled protein appears to be a novel platelet cyclic-nucleotide-binding protein. In contrast, the 49 and 55 kDa photolabelled species are probably the RI and RII regulatory subunits of cAMP-dependent protein kinase, and the 38 kDa protein(s) may be proteolytic fragment(s) of RI and/or RII.

scholarly journals Photoaffinity labelling of cyanomethaemoglobin with derivatives of tryptophan and 5-bromotryptophan

1995 ◽  
Vol 308 (1) ◽  
pp. 251-260 ◽  
Author(s):  
M Li ◽  
Z Lin ◽  
M E Johnson
Keyword(s):  
Amino Acid ◽  
Binding Sites ◽  
Tryptic Peptide ◽  
Fast Atom Bombardment ◽  
Binding Mode ◽  
Reversed Phase ◽  
Reversed Phase Hplc ◽  
Photoaffinity Labelling ◽  
Derivatives Of ◽  
Fast Atom Bombardment Ms

Tryptophan and 5-bromotryptophan (5-BrTrp) are relatively potent inhibitors of sickle-haemoglobin polymerization. The binding sites of these compounds to normal and sickle haemoglobin (HBA and HBS) have been suggested, but not firmly established, through the use of spin-labelled derivatives and/or computer modeling. In the present study we approached the problem by utilizing the technique of photoaffinity labelling. The cyanomet forms of HBA and HBS were subjected to photoaffinity labelling with N alpha-(4-azidotetrafluorobenzoyl)tryptophan and N alpha-(1-ethyl-2-diazomalonyl)-5-bromotryptophan respectively. Both irradiated samples of HBA and HBS were denatured, digested with trypsin, and then separated by reversed-phase HPLC. A labelled tryptic peptide was isolated from the photolabelling of HBS with N alpha-(1-ethyl-2-diazomalonyl)-5-bromotryptophan. The peptide was identified to be Val1(alpha)-Lys7(alpha), with the label attached to Val1(alpha), by virtue of amino acid analysis and sequencing, in conjunction with fast-atom-bombardment MS. The binding mode of N alpha-(1-ethyl-2-diazomalonyl)-5-bromotryptophan is proposed and its relevance to the potency of the 5-BrTrp-based anti-sickling agents is discussed.

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