Synthesis of a fluorescent boronic acid which reversibly binds to cell walls and a diboronic acid which agglutinates erythrocytes.
AuthorsBurnett TJ, Peebles HC, Hageman JH
JournalBiochem Biophys Res Commun
PubMed ID6776951
Steady-state kinetics of the binding of beta-lactams and penicilloates to the second binding site of the Enterobacter cloacae P99 beta-lactamase.
AuthorsDryjanski M, Pratt RF
JournalBiochemistry
PubMed ID7893652
'Previous research has shown that the class C beta-lactamase of Enterobacter cloacae P99 is able to catalyze the hydrolysis and aminolysis of acyclic depsipeptides. The steady kinetics of these reactions are complicated by the presence of an additional (depsi)peptide binding site in addition to the active site [Pazhanisamy, S., & ... More
Effect of hydroxyorganoboranes on synthesis, transport and N-linked glycosylation of plasma proteins.
AuthorsGoldberger G, Paz MA, Torrelio BM, Okamoto Y, Gallop PM
JournalBiochem Biophys Res Commun
PubMed ID2823813
'Utilizing a recently developed method (Boradeption) for transferring water-insoluble hydroxyorganoborane compounds into the cells, we observed inhibition of protein synthesis by three of these compounds and inhibition of secretion of plasma proteins by four of them in human hepatoma HepG2 cells. These effects were specific in that the cell viability ... More
Carbohydrate recognition by boronolectins, small molecules, and lectins.
AuthorsJin S, Cheng Y, Reid S, Li M, Wang B,
JournalMed Res Rev
PubMed ID19291708
'Carbohydrates are known to mediate a large number of biological and pathological events. Small and macromolecules capable of carbohydrate recognition have great potentials as research tools, diagnostics, vectors for targeted delivery of therapeutic and imaging agents, and therapeutic agents. However, this potential is far from being realized. One key issue ... More
Recent advances in methods for the analysis of catecholamines and their metabolites.
AuthorsTsunoda M
JournalAnal Bioanal Chem
PubMed ID16924378
'Catecholamines, for example epinephrine, norepinephrine, and dopamine, are widely distributed and are important neurotransmitters and hormones in mammalian species. Several methods have been developed for analysis of catecholamines and related compounds. Determination of catecholamines in biological fluids has enabled us to clarify the physiological role played by these amines. Catecholamine ... More
Inhibition of subtilisin by substituted arylboronic acids.
AuthorsPhilipp M, Maripuri S
JournalFEBS Lett
PubMed ID7030786
Fluorometric measurement of glycosylated albumin in human serum.
AuthorsHayashi Y, Makino M
JournalClin Chim Acta
PubMed ID4028431
A simple and rapid fluorometric assay of glycosylated albumin was developed using dansylated phenyl boronic acid (N-(5-dimethyl amino-1-naphthalene sulfonyl)-3-aminobenzene boronic acid). The emission spectrum of the reagent changes upon binding to cis-diols present on glycosylated albumin in serum, allowing quantitation of glycosylated albumin. Results from the new procedure correlated well ... More
N-(5-dimethylaminonaphthalene-1-sulfonyl)-3-aminobenzene boronic acid as an active-site-directed fluorescent probe of lipoprotein lipase.
AuthorsVainio P
JournalBiochim Biophys Acta
PubMed ID6882771
Resonance energy transfer was used to monitor the interaction of an active-site-directed fluorescent inhibitor, N-(5-dimethylaminonaphthalene-1-sulfonyl)-3-aminobenzene boronic acid, and lipoprotein lipase (EC 3.1.1.34). The binding of this probe to the active site of lipoprotein lipase had an association constant, Ka, of 1.1 X 10(6) M-1, indicating a strong interaction. The binding ... More
Fluorometric detection of glycosphingolipids on thin-layer chromatographic plates.
AuthorsWatanabe K, Mizuta M
JournalJ Lipid Res
PubMed ID7595105
A microdetection system for glycosphingolipid analysis has been developed using 5-hydroxy-1-tetralone as the fluorescent labeling reagent. The reagents in H2SO4 permit the fluorometric detection of acidic and neutral glycosphingolipids both in test tube and on thin-layer chromatographic plates. Glycosphingolipids can be detected at concentrations as low as 5 pmol on ... More
Boradeption: a new procedure for transferring water-insoluble agents across cell membranes.
AuthorsGallop PM, Paz MA, Henson E
JournalScience
PubMed ID6178158
A new process has been developed which is called "Boradeption" to signify boronic acid--dependent phase transfer of water-insoluble agents. Highly fluorescent boronic acid dervatives, FluoroBoras, are solubilized with a physiologically compatible carrier buffer containing a receptor group for boronate adduct formation. The system can be used to stain living cells. ... More
Role of asparagine 152 in catalysis of beta-lactam hydrolysis by Escherichia coli AmpC beta-lactamase studied by site-directed mutagenesis.
AuthorsDubus A, Normark S, Kania M, Page MG
JournalBiochemistry
PubMed ID7779822
The role of asparagine 152 in the catalytic mechanism of Escherichia coli AmpC beta-lactamase has been investigated by site-directed mutagenesis. The residue has been replaced by aspartic acid, glutamic acid, histidine, and leucine. All the substitutions had similar effects on the activity toward substrates and inhibitors. The rate of substrate ... More
Beta-lactamase-catalyzed aminolysis of depsipeptides: proof of the nonexistence of a specific D-phenylalanine/enzyme complex by double-label isotope trapping.
AuthorsPazhanisamy S, Pratt RF
JournalBiochemistry
PubMed ID2684267
The steady-state kinetics of the Enterobacter cloacae P99 beta-lactamase-catalyzed aminolysis of the depsipeptide m-[[(phenylacetyl)glycyl]oxy]benzoic acid by D-phenylalanine were consistent with an ordered sequential mechanism with D-phenylalanine binding first [Pazhanisamy, S., Govardhan, C. P., & Pratt, R. F. (1989) Biochemistry (first of three papers in this issue)]. In terms of this ... More
Beta-lactamase-catalyzed aminolysis of depsipeptides: peptide inhibition and a new kinetic mechanism.
AuthorsPazhanisamy S, Pratt RF
JournalBiochemistry
PubMed ID2819040
The aminolysis of the depsipeptide m-[[(phenylacetyl)glycyl]oxy]benzoic acid (1) by D-phenylalanine, catalyzed by the beta-lactamase of Enterobacter cloacae P99, is inhibited by the product of the reaction, (phenylacetyl)glycyl-D-phenylalanine (2), by the peptide analogue of 1, m-[(phenylacetyl)-glycinamido]benzoic acid (3), and by (3-dansylamidophenyl)boronic acid. Analysis of the steady-state kinetics of the effect of ... More