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ISOLATION Of THE MITOCHONDRIAL f1-f0 ADENOSINE-TRIPHOSPHATASE BY SEPHAROSE-HEXYLAMMONIUM CHROMATOGRAPHY - PROPERTIES AND RECONSTITUTION IN LIPOSOMES

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ANALYTICAL BIOCHEMISTRY 1984年第1期142卷 215-220页

作者： DREYfUS, G CELIS, H RAMIREZ, J Departamento de Bioenergética Centro de Investigaciones en Fisiología Celular Universidad Nacional Autonoma de Mexico Apartado Postal 70-600 04510 México D.F. Mexico

Lauryl dimethylamino oxide, a zwitterionic detergent, was employed to solubilize the H+ ATPase from beef heart mitochondria. A simple preparation procedure was devised to obtain f1-f0 based on a method described to purify f1 ATPase which consists of the selective adsorption of f1 to Sepharose-hexylammonium beads. The preparation showed .apprx. 18 bands in sodium dodecyl sulfate-polyacrylamide gel electrophoresis;5 correspond to f1 subunits and the rest probably to the stalk and hydrophobic sector f0. The binding of [14C]dicyclohexylcarbodiimide to a low-molecular-weight component of this preparation was demonstrated. The f1-f0 complex was reconstituted into phospholipid vesicles which displayed ATP-Pi exchange and ATP-dependent 9-aminoacridine fluorescence quenching, both sensitive to proton channel inhibitors.

关键词： f 1 -f 0 ATPase reconstitution affinity chromatography mitochondria membrane proteins

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Acacia catechu (L.f.) Willd and Scutellaria baicalensis Georgi extracts suppress LPS-induced pro-inflammatory responses through Nf-kB, MAPK, and PI3K-Akt signaling pathways in alveolar epithelial type II cells

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PHYTOTHERAPY RESEARCH 2019年第12期33卷 3251-3260页

作者： feng, Tian Zhou, Liying Gai, Shouchang Zhai, Yumeng Gou, Nan Wang, Xingchen Zhang, Xinyu Cui, Minxuan Wang, Libin Wang, Siwang Air Force Med Univ Sch Pharm Dept Chinese Mat Med & Nat Med 169 Changlexi St Xian 710032 Shaanxi Peoples R China Shaanxi Univ Chinese Med Coll Pharm Xianyang Peoples R China Air Force Med Univ Sch Pharm Dept Med Chem & Pharmaceut Anal Xian Shaanxi Peoples R China Northwest Univ Coll Life Sci & Med Xian Shaanxi Peoples R China

Acacia catechu (L.f.) Willd (ACW) and Scutellaria baicalensis Georgi (SBG) are one of the most famous couplet Chinese medicines, widely used for treating infantile cough, phlegm, and fever caused by pulmonary infection. However, the underlying molecular mechanism of their anti-inflammatory activity has not been determined. The aim of this study was to evaluate the protective effect of this couplet Chinese medicines (ACW-SBG) on lipopolysaccharide (LPS)-induced inflammatory responses in acute lung injury (ALI) model of rats and the potential molecular mechanisms responsible for anti-inflammatory activities in alveolar epithelial type II cells (AEC-II). Standardization of the 70% ethanol extract of ACW and SBG was performed by using a validated reversed-phase high-pressure liquid chromatography method. Rats were pretreated with ACW-SBG for 7 days prior to LPS challenge. We assessed the effects of ACW-SBG on the LPS-induced production of tumor necrosis factor alpha (TNf-alpha) and interleukin 1 beta (IL-1 beta) in the bronchoalveolar lavage fluid (BALf). The wet-to-dry weight ratio was calculated, and hematoxylin and eosin staining of lung tissue was performed. Cell viability of AEC-II was measured by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide assay. Real-time quantitative reverse transcription polymerase chain reaction assay was carried out to quantify the relative gene expression of TNf-alpha and IL-1 beta in AEC-II. The western blotting analysis was executed to elucidate the expression of mediators linked to nuclear factor-kappa B (Nf-kappa B), mitogen-activated protein kinase (MAPK), and phosphatidylinositol-3 kinase-protein kinase B (PI3K-Akt) signaling pathways. ACW-SBG significantly decreased lung wet-to-dry weight ratio, ameliorated LPS-induced lung histopathological changes, and reduced the release of inflammatory mediators such as TNf-alpha and IL-1 beta in BALf. In AEC-II, we found that the expression of TNf-alpha mRNA was also inhibited by

关键词： Acacia catechu (L f ) Willd MAPKs Nf-kappa B PI3K-Akt pro-inflammatory cytokines Scutellaria baicalensis Georgi

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TWO-DIMENSIONAL GEL-ELECTROPHORESIS Of MEMBRANE-PROTEINS USING ANIONIC AND CATIONIC DETERGENTS - APPLICATION TO THE STUDY Of MITOCHONDRIAL f0-f1-ATPASE

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BIOCHIMICA ET BIOPHYSICA ACTA 1984年第2期775卷 239-245页

作者： PENIN, f GODINOT, C GAUTHERON, DC Laboratoire de Biologie et Technologie des Membranes du CNRS Université Claude Bernard de Lyon F 69622 Villeurbanne Cedex France

Polyacrylamide gel electrophoresis in the presence of a cationic detergent, tetradecyltrimethylammonium bromide (TDAB) has been compared to electrophoresis in the presence of an anionic detergent, sodium dodecyl sulfate (SDS). Although, in both systems, the peptides generally migrated as a function of their molecular weight, the TDAB electrophoresis permitted us to obtain a much better resolution of several peptides of the mitochondrial f 0 -f 1 -ATPase, especially for the α and β subunits and for the oligomycin sensitivity conferring protein (OSCP). The differences between the two electrophoretic profiles have been used to devise a new technique of two-dimensional electrophoresis using successively anionic and cationic detergents. This method could be very useful in the case of membrane proteins, which are generally soluble only in the presence of powerful ionic detergents. It has been particularly successful in resolving the small peptides of the f 0 -f 1 -ATPase which were difficult to differentiate by other techniques in one- or two-dimensional polyacrylamide gel electrophoresis.

关键词： Polyacrylamide gel electrophoresis Detergent Cationic detergent Anionic detergent Membrane protein f 0 -f 1 -ATPase (Pig heart mitochondria) SDS sodium dodecyl sulfate TDAB tetradecyltrimethylammonium bromide Bis N,N′- methylene(bis)-acrylamide TEMED N,N,N′,N′- tetramethylethylene diamine ATPase adenosine-5′-triphosphatase (EC 3.6.1.3) f 1 -ATPase pig heart mitochondrial ATPase prepared according to the procedure of Penin et al. [17] OSCP oligomycin sensitivity conferring protein [27] If 1 natural protein inhibitor of mitochondrial f 1 -ATPase [25]

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Anti-arboviral activity and chemical characterization of hispidulin and ethanolic extracts from Millingtonia hortensis L.f. and Oroxylum indicum (L.) Kurz (Bignoniaceae)

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NATURAL PRODUCT RESEARCH 2023年第4期37卷 613-617页

作者： Cardoso Reis, Adriana Cotta Valente, Gabriel Mendonca Silva, Breno de Mello de Brito Magalhaes, Cintia Lopes Kohlhoff, Markus Brandao, Geraldo Celio Univ Fed Ouro Preto Escola Farm Dept Farm Ouro Preto Brazil Univ Fed Ouro Preto Dept Ciencias Biol ICEB Ouro Preto Brazil Fundacao Oswaldo Cruz Inst Rene Rachou Lab Quim Prod Nat Bioativos Belo Horizonte MG Brazil

Millingtonia hortensis L.f. and Oroxylum indicum (L.) Kurz (Bignoniaceae) are native species from the Asian continent. They are popularly used in traditional medicine and their extracts are rich in flavonoids. In this work, ethanolic extracts of stems and leaves of these species were evaluated against the Chikungunya, Zika and Mayaro virus. The extracts were subjected to analysis by ultra-efficient liquid chromatography coupled to mass spectrometry. Additionally, M. hortensis leaves extract was fractionated, leading to the isolation of hispidulin. Anti-arboviral activity against the three viruses was detected for M. hortensis leaves extract with EC50 ranging from 37.8 to 134.1 mu g/mL and for O. indicum stems extract with EC50 ranging from 18.6 to 55.9 mu g/mL. Hispidulin inhibited viral cytopathic effect of MAYV (EC50 value 32.2 mu M) and CHIKV (EC50 value 78.8 mu M). In LC-DAD-ESI-MS/MS analysis we characterized 25 flavonoids confirming once again the presence of these substances in extracts of these species.

关键词： 6-methyl-scutellarein Chikungunya virus Mayaro virus antiviral Millingtonia hortensis L f Oroxylum indicum (L ) Kurz Bignoniaceae

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IDENTIfICATION Of A MUTATION IN ESCHERICHIA-COLI f1-ATPASE BETA-SUBUNIT CONfERRING RESISTANCE TO AUROVERTIN

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fEBS LETTERS 1989年第1-2期253卷 269-272页

作者： LEE, RSf PAGAN, J SATRE, M VIGNAIS, PV SENIOR, AE Department of Biochemistry Box 607 University of Rochester Medical Center Rochester NY 14642 USA

A mutation conferring aurovertin resistance on Escherichia coli f 1 -ATPase was identified as R398 → in the f 1 β-subunit. β-subunit from the mutant doe not bind aurovertin; therefore our results suggest the region of sequence around residue β-398 is involved in aurovertin binding. Since nucleotide and aurovertin binding to isolated β-subunit are not mutually exclusive, the data further suggest that the β-subunit catalytic nucleotide-binding domain does not include residue 398. The mutation prevented aurovertin inhibition of ATPase at pH 6 and 8.5, implying charge on the arginine side-chain is not a major determinant of aurovertin binding or that the p K of R398 is shifted due to a peculiar environment. The equivalent residue is usually arginine in f 1 β-subunits of different species; notably in the aurovertin-insensitive thermophilic bacterium PS3 f 1 -ATPase, this residue is phenylalanine.

关键词： Aurovertin resistance f 1 -ATPase β-subunit Mutation

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TRYPSIN CLEAVAGE Of THE ALPHA-SUBUNIT Of BEEf-HEART f1-ATPASE ABOLISHES ATP SYNTHESIS AND ATP-DRIVEN ENERGY-TRANSDUCTION CAPABILITIES

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BIOCHIMICA ET BIOPHYSICA ACTA 1981年第1期638卷 120-124页

作者： SKERRETT, KJ WISE, JG LATCHNEY, LR SENIOR, AE Department of Biochemistry Box 607 University of Rochester Medical Center Rochester NY 14642 U.S.A.

Previous work has shown that mild trypsin treatment eliminates energy-transduction capability and tight (non-exchangeable) nucleotide binding in beef heart mitochondrial f1-ATPase. The structural change brought about by trypsin was, however, too subtle to be identified by 1-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis [SDS-PAGE] and was not defined. In this work 2-dimensional electrophoresis (isoelectric focusing then SDS-PAGE) was applied to the problem, and it was determined that the .alpha.-subunit of f1 is altered by the mild trypsin treatment, whereas no change was detected in .beta.-, .gamma.-, .delta.- or .epsilon.-subunits. Binding of ADP to the trypsin-treated f1 was compared to binding to control enzyme over a range of 0-40 .mu.M ADP in a 30 min incubation period. There was no difference between the 2 enzymes, KdADP in Mg2+-containing buffer was about 2 .mu.M in each. Since the tight (nonexchangeable) sites are abolished in trypsin-treated f1, this shows that tight exchangeable ADP-binding sites are different from the tight nonexchangeable ADP-binding sites. There was no effect of trypsin cleavage of the .alpha.-subunit on .beta.-subunit conformation as judged by aurovertin fluoresence studies. The cleavage of the .alpha.-subunit which occurred as judged to occur very close to the C- or N-terminus of the subunit and constitutes therefore a small and specific chemical modification which abolishes overall function in f1 but leaves partial functions intact.

关键词： f 1 -ATPase ATP synthesis Energy transduction Trypsin cleavage (Beef heart mitochondria, α-Subunit) ASU-particles mitochondrial inner membrane vesicles depleted of f 1 by sequential exposure to NH 3 sonication gel filtration and urea SDS sodium dodecyl sulfate

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SYNTHESIS Of A PHOTOAffINITY-SPIN-LABELED DERIVATIVE Of ATP AND ITS 1ST APPLICATION TO f1-ATPASE

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fEBS LETTERS 1988年第2期227卷 107-109页

作者： VOGELCLAUDE, P SCHAfER, G TROMMER, WE UNIV KAISERSLAUTERN FACHBEREICH CHEMERWIN SCHRODINGER STRD-6750 KAISERSLAUTERNFED REP GER MED HSCH LUBECK INST BIOCHEMD-2400 LUBECKFED REP GER

The synthesis of an ATP derivative is described, in which a spin-label is attached to the 3′-position of the ribose moiety and an azido group to C8 of the adenine ring (SL-N 3 -ATP). Irradiation of this compound at 350 nm generates a nitrene, which will react with any functional group in its vicinity. SL-N 3 -ATP exhibits a strongly immobilized ESR spectrum in a complex with f 1 -ATPase from beef heart mitochondria. It was covalently incorporated into this enzyme. SL-N 3 -ATP may be employed in ESR investigations under conditions in which non-covalent interactions are too weak for motionally restricted species to be easily observed.

关键词： f 1 -ATPase Spin-labeled ATP Photoaffinity-spin-labeled ATP N 3 -ATP the 8-azido derivative of ATP SL-ATP or SL-N 3 -ATP C3′-(2,2,5,5-tetramethyl-3-pyrroline-1-oxyl-3-carboxylic acid ester) of ATP and N 3 -ATP, respectively HPLC high-performance liquid chromatography TLC thin-layer chromatography

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N-TERMINAL AMINO-ACID SEQUENCE Of CYTOCHROME-f fROM SPIRULINA-PLATENSIS

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PHYTOCHEMISTRY 1976年第5期15卷 815-816页

作者： SANDERSON, S HASLETT, BG BOULTER, D UNIV DURHAM DEPT BOTDURHAM DH1 3LEENGLAND

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INTERACTIONS AND EffECTS Of 2-HYDROXY-5-NITROBENZYL BROMIDE ON THE BOVINE HEART MITOCHONDRIAL f(1)-ATPASE

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INTERNATIONAL JOURNAL Of BIOCHEMISTRY 1993年第9期25卷 1269-1275页

作者： BARACCA, A BAROGI, S LENAZ, G SOLAINI, G UNIV & PERFEZIONAMENTO S ANNA SCUOLA SUPERVIA CARDUCCI 40I-56100 PISAITALY UNIV BOLOGNA DEPT BIOCHEM GIOVANNI MORUZZII-40126 BOLOGNAITALY

1. The f1-ATPase from bovine heart mitochondria was shown to chemically react and to absorb 2-hydroxy-5-nitrobenzyl bromide (HNB) with changes in catalytic properties. 2. The treatment of the enzyme with HNB at concentrations below 0.5 mM resulted in an increase of V(m) and in an unchanged K(m). Above 0.5mM HNB elicited a concentration-dependent inhibition of f1. 3. HNB was found tightly bound to the enzyme epsilon-subunit whose tryptophan residue resulted modified. 4. The f1 activation appears the consequence of the covalent binding of the reagent to the enzyme, whilst inhibition results from non-covalent, reversible binding. 5. The possibility that the epsilon-subunit of mitochondrial f1-ATPase may influence the functional or regulating domain of the enzyme is discussed.

关键词： f 1 , f 1 ,-ATPase a catalytic component of the proton-translocating ATPase complex from bovine heart mitochondria (EC 3.6.1.34) f 0 , proton channel portion of the ATP synthase complex If 1 natural inhibitor protein HNB 2-hydroxy-5-nitrobenzyl bromide HPLC high performance liquid chromatography Trp tryptophan pyruvate kinase (EC 2.7.1.40) lactate dehydrogenase (EC 1.1.1.27)

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THE MITOCHONDRIAL ATP SYNTHASE Of TRYPANOSOMA-BRUCEI - ISOLATION AND CHARACTERIZATION Of THE INTACT f1 MOIETY

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MOLECULAR AND BIOCHEMICAL PARASITOLOGY 1990年第1期43卷 125-132页

作者： WILLIAMS, N fRANK, PH Uniformed Services University of the Health Sciences Department of Biochemistry Bethesda MD 20814-4799.

This report describes the first isolation and molecular characterisation of the mitochondrial f1-ATPase from Trypanosoma brucei. The isolation procedure utilized is a modified chloroform extraction procedure. In contrast to earlier reports on the f1-ATPase from other trypanosomatids, the f1-ATPase we have isolated from the procyclic form of T. brucei a complex composed of five distinct subunits. Apparent molecular weights of these subunits are 55000[.alpha.], 42000 [.beta.], 32000 [.gamma.), 22000 [.delta.], and 17000 [.epsilon.]. The f1 moiety which possesses the active site of the H+-ATPase has an ATPase activity in the standard Tris-HCl coupled enzyme assay with Vmax of 22.96 .*** min-1 (mg protein)-1 and a Km value of 0.60 mM. This ATPase activity is cold labile and is not susceptible to oligomycin inhibition as is the membrane bound enzyme. Upon reconstitution with f1-ATPase depleted membranes (urea particles) the ATPase regains oligomycin sensitivity to the same extent as that found in the intact inner membrane vesicles. ATP synthesis is also restored to these particles upon reconstitution with f1. These results indicate that this f1-ATPase as isolated is intact with respect to all the critical H+-ATPase functions.

关键词： Bioenergetics Trypanosoma brucei f 1 -ATPase Purification Reconstitution Kinetics PEP phosphoenolpyruvate LDH lactate dehydrogenase PK pyruvate kinase BSA bovine serum albumin SDS sodium dodecyl sulfate TEMED N , N , N ′, N ′-tetramethylenediamine

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