Nucleotide-induced movements in the myosin head near the converter region.
AuthorsPliszka B, Karczewska E, Wawro B
JournalBiochim Biophys Acta
PubMed ID10962092
'Structural changes in subfragment 1 of skeletal muscle myosin were investigated by cross-linking trypsin-cleaved S1 with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide. In the absence of nucleotide the alkali light chains are cross-linked to the 27 kDa heavy chain fragment; the presence of MgATP reduces the efficiency of this reaction. On the other hand, MgATP ... More
Sensitive method for the analysis of phospholipid subclasses and molecular species as 1-anthroyl derivatives of their diglycerides.
AuthorsRamesha CS, Pickett WC, Murthy DV
JournalJ Chromatogr
PubMed ID2793981
'A sensitive high-performance liquid chromatographic (HPLC) method for the separation and quantitation of phospholipid subclasses and molecular species has been developed. Phospholipids for analysis are hydrolyzed to the diradyl glycerols (DGs) with phospholipase C and the resulting DGs reacted with a molar excess of 1-anthroyl nitrile in the presence of ... More
Chemical identification of serine 181 at the ATP-binding site of myosin as a residue esterified selectively by the fluorescent reagent 9-anthroylnitrile.
AuthorsHiratsuka T, Katoh T
JournalJ Biol Chem
PubMed ID12805386
'The esterification reagent 9-anthroylnitrile (ANN) reacts with a serine residue in the NH2-terminal 23-kDa peptide segment of myosin subfragment-1 heavy chain to yield a fluorescent S1 derivative labeled by the anthroyl group (Hiratsuka, T. (1989) J. Biol. Chem. 264, 18188-18194). The labeling was highly selective and accelerated by nucleotides. In ... More
Binding between maleimidobenzoyl-G-actin and myosin subfragment 1.
AuthorsHozumi T
JournalBiochemistry
PubMed ID1390764
'It is well known that the structural interactions between S-1 moieties of myosin molecules ("cross bridges") and actin molecules in polymerized ("F") form are thought to underlie muscle contraction. It is surmised that such interactions are unitary (actin:S-1 = 1:1), but actual demonstration thereof is handicapped by intrinsic properties of ... More
Quantitation of monohydroxy fatty acids by high-performance liquid chromatography with fluorescence detection.
AuthorsMetori A, Ogamo A, Nakagawa Y
JournalJ Chromatogr
PubMed ID8150863
'A high-performance liquid chromatographic (HPLC) procedure for the separation of hydroxyeicosatetraenoic acids (HETEs) and hydroxyoctadecanoic acids (HODEs) after derivatization of the hydroxy group with 1-anthroylnitrile is described. Anthroyl esters of HETEs were separated from those of HODEs by reversed-phase HPLC. The positional isomers of the HETEs and HODEs were well ... More
Modulation of mediator precursors by changes in essential fatty acid composition.
AuthorsPickett WC, Ramesha C
JournalAdv Prostaglandin Thromboxane Leukot Res
PubMed ID2526546
Determination of aloesin in plasma by high-performance liquid chromatography as fluorescent 9-anthroyl derivative.
AuthorsKim KH, Lee JG, Park JH, Shin YG, Lee SK, Cho TH, Oh ST
JournalArch Pharm Res
PubMed ID9868532
A sensitive high-performance liquid chromatographic (HPLC) method for the determination of aloesin in plasma was developed. After solid-phase extraction from plasma and derivatization of aloesin and compound AD-1, which was prepared from aloesin as a internal standard, with 9-anthroylnitrile in the presence of quinuclidine, the derivatives were separated on a ... More
Separation of carnitine enantiomers as the 9-anthroylnitrile derivatives and high-performance liquid chromatographic analysis on an ovomucoid-conjugated column.
AuthorsTakahashi M, Terashima K, Nishijima M, Kamata K
JournalJ Pharm Biomed Anal
PubMed ID8877865
9-Anthroylnitrile was used as an achiral reagent for the derivatization of carnitine. The reagent forms UV-absorbing derivatives with the hydroxyl groups of carnitine enantiomers under very mild conditions. The derivatives were separated by high-performance liquid chromatography on an ovomucoid-conjugated column with a mobile phase of acetonitrile-20 mM KH2PO4 (adjusted to ... More
9-Anthroylnitrile binding to serine-181 in myosin subfragment 1 as revealed by FRET spectroscopy and molecular modeling.
AuthorsSzarka K, Bódis E, Visegrády B, Nyitrai M, Kilár F, Somogyi B
JournalBiochemistry
PubMed ID11732899
It has been shown that one of the 12 serine residues within the 23 kDa segment of myosin subfragment 1 can be covalently modified with a fluorescent probe 9-anthroylnitrile (ANN) [Hiratsuka, T. (1989) J. Biol. Chem. 264 (30), 18188-18194]. To identify the exact binding site of the probe, the distances ... More
Determination of T-2 toxin in cereal grains by liquid chromatography with fluorescence detection after immunoaffinity column clean-up and derivatization with 1-anthroylnitrile.
AuthorsPascale M, Haidukowski M, Visconti A
JournalJ Chromatogr A
PubMed ID12650258
1-Anthroylnitrile (1-AN) has been shown to be an efficient labelling reagent for the determination of T-2 toxin (T-2) by high-performance liquid chromatography (HPLC)-fluorescence detection. This reaction has been used to develop a sensitive, reproducible and accurate method for the determination of T-2 in wheat, corn, barley, oats, rice and sorghum. ... More
Determination of farnesyl pyrophosphate in dog and human plasma by high-performance liquid chromatography with fluorescence detection.
AuthorsSaisho Y, Morimoto A, Umeda T
JournalAnal Biochem
PubMed ID9324945
A nonradioisotopic method has been developed for the determination of all-trans-farnesyl pyrophosphate (FPP), the common intermediate at the branch point of the biosynthesis of cholesterol and nonsterol end products, in dog and human plasma. FPP was cleaved to the parent alcohol, farnesol, by the direct addition of alkaline phosphatase to ... More
Molecular movements in the actomyosin complex: F-actin-promoted internal cross-linking of the 25- and 20-kDa heavy chain fragments of skeletal myosin subfragment.
AuthorsBertrand R, Derancourt J, Kassab R
JournalBiochemistry
PubMed ID1457419
We describe, for the first time, the F-actin-promoted changes in the spatial relationship of strands in the NH2-terminal 25-kDa and COOH-terminal 20-kDa heavy chain fragments of the skeletal myosin subfragment 1 (S-1), detected by their exclusive chemical cross-linking in the rigor F-actin-S-1 complex with m-maleimidobenzoic acid N-hydroxysuccinimide ester (MBS). Quantitative ... More
Nucleotide-induced specific fluorescent labeling of the 23-kDa NH2-terminal tryptic peptide of myosin ATPase by the serine-reactive reagent 9-anthroylnitrile.
AuthorsHiratsuka T
JournalJ Biol Chem
PubMed ID2530221
The fluorescent reagent 9-anthroylnitrile (ANN) reacted preferentially with serine among various amino acids tested. When the myosin subfragment-1 (S-1) was incubated with ANN, the 9-anthroyl (AN) group was covalently incorporated into the S-1 heavy chain. The incorporation of the AN group was enhanced by the presence of ATP and ADP. ... More
Studies on steroids. CLXXXVII. Determination of serum bile acids by high-performance liquid chromatography with fluorescence labeling.
AuthorsGoto J, Saito M, Chikai T, Goto N, Nambara T
JournalJ Chromatogr
PubMed ID6630379
A method for the simultaneous determination of bile acids in serum by high-performance liquid chromatography (HPLC) with fluorescence labeling is described. The bile acid fraction was obtained from a serum specimen by passing it through a BondElut cartridge. Bile acids were derivatized quantitatively into the fluorescent compounds through the hydroxyl ... More
Structure of the 265-kilodalton complex formed upon EDC cross-linking of subfragment 1 to F-actin.
AuthorsAndreeva AL, Andreev OA, Borejdo J
JournalBiochemistry
PubMed ID8268172
The conventional model of force generation in muscle requires the presence of at least two different contact areas between the myosin head (S1) and the actin filament. It has been found that S1 has two sites available for carbodiimide cross-linking, but it is generally believed that the myosin head can ... More
Conformational changes in the 23-kilodalton NH2-terminal peptide segment of myosin ATPase associated with ATP hydrolysis.
AuthorsHiratsuka T
JournalJ Biol Chem
PubMed ID2146263
A fluorophore, 9-anthroyl (AN) group, was covalently incorporated into the 23-kDa NH2-terminal peptide segment of myosin subfragment-1 (S-1) (Hiratsuka, T. (1989) J. Biol. Chem. 264, 18188-18194). The fluorescent S-1 derivative (AN-S-1) was utilized to detect conformational changes in the 23-kDa segment associated with ATP hydrolysis of S-1. The extrinsic fluorescence ... More
Specific cross-linking of the SH1 thiol of skeletal myosin subfragment 1 to F-actin and G-actin.
AuthorsBettache N, Bertrand R, Kassab R
JournalBiochemistry
PubMed ID1731896
Recently, we reported that (maleimidobenzoyl)-G-actin (MBS-G-actin), which was resistant to the salt and myosin subfragment 1 (S-1) induced polymerizations, reacts reversibly and covalently in solution with the S-1 heavy chain at or near the strong F-actin binding region [Bettache, N., Bertrand, R., & Kassab, R. (1989) Proc. Natl. Acad. Sci. ... More
Transmission of ADP.vanadate-induced conformational changes to three peptide segments of myosin subfragment-1.
AuthorsHiratsuka T
JournalJ Biol Chem
PubMed ID2229042
In order to study the conformational changes associated with formation of the stable ternary complex of myosin subfragment-1 (S-1) with ADP and orthovanadate (Vi), S-1 was fluorescently labeled with 9-anthroylnitrile, 4-fluoro-7-nitrobenz-2-oxa-1,3-diazole, and 5-(iodoacetamido) fluorescein at the 23-, 50-, and 20-kDa peptide segments of S-1, respectively (Hiratsuka, T. (1989) J. Biol. ... More
Simultaneous determination of glucocorticoids in plasma or urine by high-performance liquid chromatography with precolumn fluorimetric derivatization by 9-anthroyl nitrile.
AuthorsShibata N, Hayakawa T, Takada K, Hoshino N, Minouchi T, Yamaji A
JournalJ Chromatogr B Biomed Sci Appl
PubMed ID9551805
A new method for simultaneous determination of glucocorticoids (GCs) in plasma or urine by high-performance liquid chromatography (HPLC) with fluorimetric detection has been developed. Following extraction with ethyl acetate using a reversed-phase disposable cartridge, the six GCs [cortisol (F), cortisone (E), prednisolone (PL), prednisone (PN), 6beta-hydroxycortisol (6beta-OHF) and 6beta-hydroxyprednisolone (6beta-OHP)] ... More
A myosin head can interact with two chemically modified G-actin monomers at ATP-modulated multiple sites.
AuthorsArata T
JournalBiochemistry
PubMed ID8973176
It has been reported that chemically modified [with m-maleimidobenzoic acid N-hydroxysuccinimide ester (MBS)] actin maintains its monomeric form and retains the ability to bind (and make chemical cross-links) to myosin head [Bettache, N., Bertrand, R., & Kassab, R. (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 6028-6032; Arata, T. (1991) J. ... More
Effect of nucleotides and actin on the intramolecular cross-linking of myosin subfragment-1.
AuthorsBlotnick E, Muhlrad A
JournalBiochemistry
PubMed ID8204621
The heavy chain of myosin subfragment-1 (S1) is cleaved by limited trypsinolysis into three fragments, 27, 50, and 20 kDa--aligned in this order from the N-terminus. The tertiary structure of the molecule is essentially not affected by trypsinolysis. The spatial relations between the various regions of the molecule and the ... More
Fluorescence polarization study of the rigor complexes formed at different degrees of saturation of actin filaments with myosin subfragment-1.
AuthorsAndreev OA, Takashi R, Borejdo J
JournalJ Muscle Res Cell Motil
PubMed ID7499476
A serine residue located in the active site of myosin head (S1) was labelled by 9-anthroylnitrile, an amino group located in the central domain of S1 was labelled by 7-diethylamino-3-(4'-isothio-cyanato-phenyl)-4-methylcoumari n, a cysteine residue located near the C-terminus of S1 was labelled by 5-[2-((iodoacetyl)-amino)ethyl]-amino-naphthalene-1-sulfonic acid (1,5-IAEDANS) and a cysteine residue ... More