Identification of the C-terminal part of Bordetella dermonecrotic toxin as a transglutaminase for rho GTPases.
AuthorsSchmidt G,Goehring UM,Schirmer J,Lerm M,Aktories K
JournalThe Journal of biological chemistry
PubMed ID10542213
Enkephalin analogs. Introduction of sterochemical constraints, metal binding sites and fluorescent groups.
AuthorsNagaraj R, Sudha TS, Shivaji S, Balaram P
JournalFEBS Lett
PubMed ID499510
Physical and biological properties of fluorescent dansylated bile salt derivatives: the role of steroid ring hydroxylation.
AuthorsCrawford JM, Lin YJ, Teicher BA, Narciso JP, Gollan JL
JournalBiochim Biophys Acta
PubMed ID1892892
'The hydroxyl groups of bile salts play a major role in determining their physical properties and physiologic behavior. To date, no fluorescent bile salt derivatives have been prepared which permit evaluation of the functional role of the steroid ring. We have prepared five fluorescent cholanoyl derivatives using a dansyl-ethylene diamine ... More
Modification of oligosaccharide antenna flexibility induced by exoglycosidase trimming.
AuthorsRice KG, Wu P, Brand L, Lee YC
JournalBiochemistry
PubMed ID8343515
'We have investigated the solution conformation of a triantennary glycopeptide using resonance energy transfer [Rice et al. (1991) Biochemistry 30, 6646-6655]. Triantennary glycopeptide was derivatized with a donor fluorophore on the N-terminus and with an acceptor fluorophore attached individually to each terminal galactose residue, resulting in three isomeric donor-acceptor pairs. ... More
Conformational studies of glycopeptides by energy transfer. Introduction of fluorophore at specific branches of biantennary glycopeptides.
AuthorsLee KB, Lee YC
JournalJ Biol Chem
PubMed ID8576139
'Biantennary glycopeptides from bovine fibrinogen were fluorescence labeled at each branch specifically for conformational studies by fluorescence energy transfer. Glycopeptides (by Pronase digestion) were separated by anion-exchange chromatography based on the degree of sialylation. The major monosialyl biantennary glycopeptides (see below) were used as substrates for galactose oxidase and periodate ... More
Intermolecular coupling between loop 38-52 and the C-terminus in actin filaments.
AuthorsKim E, Reisler E
JournalBiophys J
PubMed ID8889166
'The recently reported structural connectivity in F-actin between the DNase I binding loop on actin (residues 38-52) and the C-terminus region was investigated by fluorescence and proteolytic digestion methods. The binding of copper to Cys-374 on F- but not G-actin quenched the fluorescence of dansyl ethylenediamine (DED) attached to Gin-41 ... More
Influence of core fucosylation on the flexibility of a biantennary N-linked oligosaccharide.
AuthorsStubbs HJ, Lih JJ, Gustafson TL, Rice KG
JournalBiochemistry
PubMed ID8547276
'Fluorescence energy transfer was used to study the conformation of each antenna of a complex biantennary oligosaccharide. A core fucosylated biantennary oligosaccharide was converted to a glycosylamine which allowed coupling of a naphthyl donor fluorophore directly to the reducing-end GlcNAc 1. After generating an aldehyde at C-6 of residue 6 ... More
Myosin-induced changes in F-actin: fluorescence probing of subdomain 2 by dansyl ethylenediamine attached to Gln-41.
AuthorsKim E, Miller CJ, Motoki M, Seguro K, Muhlrad A, Reisler E
JournalBiophys J
PubMed ID8785300
'Actin labeled at Gln-41 with dansyl ethylenediamine (DED) via transglutaminase reaction was used for monitoring the interaction of myosin subfragment 1 (S1) with the His-40-Gly-42 site in the 38-52 loop on F-actin. Proteolytic digestions of F-actin with subtilisin and trypsin, and acto-S1 ATPase measurements on heat-treated F-actin revealed that the ... More
Fluorescent labeling of the carbohydrate moieties of human chorionic gonadotropin and alpha 1-acid glycoprotein.
AuthorsIngham KC, Brew SA
JournalBiochim Biophys Acta
PubMed ID6271241
'A method for covalent attachment of a fluorescent molecule to the carbohydrate moieties of glycoproteins is described. The glycoproteins were oxidized with periodate under mild conditions selective for sialic acid (Van Lenten, L. and Ashwell, G. (1971) J. Biol. Chem. 246, 1889--1894). The resulting aldehydes were condensed with either dansylhydrazine, ... More
Fluorescent probe studies of mixed micelles of phospholipids and bile salts. Effect of cholesterol incorporation.
AuthorsNarayanan R, Paul R, Balaram P
JournalBiochim Biophys Acta
PubMed ID7370247
'The binding of the fluorescent alkylamines, N-(2-aminoethyl)-5-dimethyl-amino-1-naphthalene sulfonamide, N-(5-aminopentyl)-5-dimethylamino-1-naphthalene sulfonamide (dansyl cadaverine) and N-(10-aminodecyl)-5-dimethylamino-1-napthalene sulfonamide with phospholipid and phospholipid-deoxycholate micelles, has been shown to increase with the length of the alkyl spacer chain. The probes bind more effectively to micelles containing unsaturated phospholipids and do not interact strongly with bile ... More
Fluorescent enkephalin derivatives with biological activity.
Labeling of the glycoprotein subunit of (Na,K)ATPase with fluorescent probes.
AuthorsLee JA, Fortes PA
JournalBiochemistry
PubMed ID2983755
'Sodium plus potassium activated adenosinetriphosphatase [(Na,K)ATPase] is composed of a catalytic subunit (alpha) and a glycoprotein subunit (beta) of unknown function. A method has been developed to label the beta subunit of purified dog kidney (Na,K)ATPase with fluorescent probes. The method consists of oxidation of beta-subunit oligosaccharides, reaction of the ... More
Conformational changes in subdomain 2 of G-actin: fluorescence probing by dansyl ethylenediamine attached to Gln-41.
AuthorsKim E, Motoki M, Seguro K, Muhlrad A, Reisler E
JournalBiophys J
PubMed ID8580345
'Gln-41 on G-actin was specifically labeled with a fluorescent probe, dansyl ethylenediamine (DED), via transglutaminase reaction to explore the conformational changes in subdomain 2 of actin. Replacement of Ca2+ with Mg2+ and ATP with ADP on G-actin produced large changes in the emission properties of DED. These substitutions resulted in ... More
Application of fluorescence resonance energy transfer to analyze carbohydrates.
AuthorsRice KG
JournalAnal Biochem
PubMed ID11673877
Preparation of fluorescent glycoconjugates for energy transfer studies.
AuthorsRice KG
JournalMethods Enzymol
PubMed ID7534863
Syntheses, properties, and use of fluorescent N-(5'-phospho-4'-pyridoxyl)amines in assay of pyridoxamine (pyridoxine) 5'-phosphate oxidase.
AuthorsDePecol ME, McCormick DB
JournalAnal Biochem
PubMed ID7362038
Disappearance of energy-transfer as a tool for fluorimetric study of the degradation of enkephalins by aminopeptidase activity from mouse brain.
Fibrin-stabilizing factor inhibitors. 3. Sulphonamides related to monodansylcadaverine.
AuthorsNilsson JL, Stenberg P, Ljunggren C, Eriksson O, Lundén R
JournalActa Pharm Suec
PubMed ID5159519
Interaction and thermal stability of fluorescent labeled derivatives of thrombin and antithrombin III.
AuthorsAtha DH, Brew SA, Ingham KC
JournalBiochim Biophys Acta
PubMed ID6696918
Derivatives of human thrombin and antithrombin III with fluorescent labels covalently attached to their carbohydrate moieties were prepared by reaction of periodate-oxidized proteins with amino derivatives of dansyl, fluorescein and pyrene. The labeled derivatives retained full biological activity, including their ability to form stable enzyme-inhibitor complexes, a reaction whose rate ... More
Transglutaminase-induced cross-linking between subdomain 2 of G-actin and the 636-642 lysine-rich loop of myosin subfragment 1.
AuthorsEligula L, Chuang L, Phillips ML, Motoki M, Seguro K, Muhlrad A
JournalBiophys J
PubMed ID9533706
G-actin was covalently cross-linked with S1 in a bacterial transglutaminase-catalyzed reaction. The cross-linking sites were identified with the help of fluorescent probes and limited proteolysis as the Gln-41 on the DNase I binding loop of subdomain 2 in G-actin and a lysine-rich loop (residues 636-642) on the S1 heavy chain. ... More
Sequence 18-29 on actin: antibody and spectroscopic probing of conformational changes.
AuthorsAdams SB, Reisler E
JournalBiochemistry
PubMed ID7981202
Experimental evidence for the involvement of the 18-29 site within actin subdomain-1 in the actomyosin weak binding interface includes the inhibition of actomyosin ATPase activity by specific peptide antibodies [Adams, S., & Reisler, E. (1993) Biochemistry 32, 5051-5056] and by the Dictyostelium actin mutant D24H/D25H [Johara, M., et al. (1993) ... More
Extrinsic signals for monitoring the association reaction of proteins as introduced by fluorescent and non-fluorescent labels.
AuthorsBösterling B, Engel J, Steinemann A, Schramm HJ
JournalHoppe Seylers Z Physiol Chem
PubMed ID11168
Two known dansyl labels (I, II) and 5-[2-(iodoacetamido)ethylamino]-1-naphthalene-sulfonic acid (III) and three new azo-dyes (IV - VI) were covalently attached to alpha-chymotrypsin and to basic pancreatic trypsin inhibitor by four different reactive groups. In order to protect the contact region of the proteins the complex of the two proteins was ... More
Divalent cation-, nucleotide-, and polymerization-dependent changes in the conformation of subdomain 2 of actin.
AuthorsMoraczewska J, Wawro B, Seguro K, Strzelecka-Golaszewska H
JournalBiophys J
PubMed ID10388764
Conformational changes in subdomain 2 of actin were investigated using fluorescence probes dansyl cadaverine (DC) or dansyl ethylenediamine (DED) covalently attached to Gln41. Examination of changes in the fluorescence emission spectra as a function of time during Ca2+/Mg2+ and ATP/ADP exchange at the high-affinity site for divalent cation-nucleotide complex in ... More
Solution conformations of a biantennary glycopeptide and a series of its exoglycosidase products from sequential trimming of sugar residues.
AuthorsWu P, Lee KB, Lee YC, Brand L
JournalJ Biol Chem
PubMed ID8576140
Linkages between sugar residues in branched oligosaccharides exhibit various degrees of flexibility. This flexibility, together with other forces, determines the overall solution conformation of oligosaccharides. We used the method of time-resolved resonance energy transfer to study the solution conformations of a biantennary glycopeptide and its partially trimmed products by exoglycosidases. ... More
Interaction of myosin subfragment 1 with fluorescent ribose-modified nucleotides. A comparison of vanadate trapping and SH1-SH2 cross-linking.
AuthorsCremo CR, Neuron JM, Yount RG
JournalBiochemistry
PubMed ID2110475
The environment near the ribose binding site of skeletal myosin subfragment 1 (S1) was investigated by use of two adenosine 5'-diphosphate analogues with fluorescent groups attached at the 2'- and 3'-hydroxyls of the ribose ring. We have compared steady-state and time-resolved fluorescent properties of the reversibly bound S1-nucleotide complexes and ... More
Structural effects of cofilin on longitudinal contacts in F-actin.
AuthorsBobkov AA, Muhlrad A, Kokabi K, Vorobiev S, Almo SC, Reisler E
JournalJ Mol Biol
PubMed ID12419261
Structural effects of yeast cofilin on skeletal muscle and yeast actin were examined in solution. Cofilin binding to native actin was non-cooperative and saturated at a 1:1 molar ratio, with K(d)<or=0.05 microM for both CaATP-G-actin and F-actin. Cofilin binding enhanced the fluorescence of dansyl ethylenediamine (DED) attached to Gln41 on ... More