当前位置： SCI文献检索 > BIOCHEMISTRY期刊下所有文献 > Interconverting receptor states at 4 degrees C for the neutrophil N-formyl peptide receptor.

Interconverting receptor states at 4 degrees C for the neutrophil N-formyl peptide receptor.

Abstract：

:With the aid of high time resolution kinetic data extracted from a flow cytometer, we determined that there are two N-formyl peptide receptor states for human neutrophils at 4 degrees C: a low affinity and a high affinity state. Competitive binding of FMLP, FNLP, and t-BOC with FNLPNTL-FL revealed different kinetic rate constants for two distinct reactions that control the lifetime of the low affinity ligand-receptor complex. For these ligands, the rate constant for dissociation of ligand from the low affinity receptor state (the first reaction) ranges in order of magnitude from 10(-2) to 1 s-1, and the conversion rate constant from the low affinity receptor state to the high affinity receptor state (the second reaction) ranges from 10(-4) to 10(-2) s-1. The antagonist t-BOC differed most significantly from the three agonists by having an association rate constant for the low affinity receptor on the order of 10(5) M-1 s-1; the value for all three agonists was on the order of 10(7) M-1 s-1. Characterization of the receptor conversion at 4 degrees C revealed that it is irreversible (or very slow) and independent of Gi protein and that neither receptor state is a form of receptor precoupled to Gi protein. The affinity conversion and the dissociation characteristics of each receptor state determine the duration of the signaling complex and may contribute to differences in ligand efficacy.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Hoffman JF,Keil ML,Riccobene TA,Omann GM,Linderman JJ

doi

10.1021/bi961088p

subject

Has Abstract

pub_date

1996-10-08 00:00:00

pages

13047-55

issue

40

eissn

0006-2960

issn

1520-4995

pii

bi961088p

journal_volume

35

pub_type

杂志文章

相关文献

BIOCHEMISTRY文献大全
  • Studies on the hydrolytic properties of (serine) carboxypeptidase Y.

    abstract：:The activity of serine carboxypeptidases is dependent on a catalytic triad, an oxyanion hole, and a binding site equivalent to those found in the serine endopeptidases. The action of carboxypeptidase Y on substrates containing amino acids, alcohols, and amines as leaving groups is described. It is demonstrated that th...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi952758e

    authors： Stennicke HR,Mortensen UH,Breddam K

    更新日期：1996-06-04 00:00:00

  • Comparisons of redox kinetics of methemerythrin and mu-sulfidomethemerythrin. Implications for interactions with cytochrome b5.

    abstract：:We have examined the effects on redox kinetics of changing the reduction potential of the mu-oxo-bridged binuclear iron center in octameric hemerythrin (Hr) from Phascolopsis gouldii. The opportunity to examine such effects is provided by the availability of mu-sulfidomethemerythrin (mu-S2-metHr), whose [Fe(III),Fe(II...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi00400a033

    authors： Pearce LL,Utecht RE,Kurtz DM Jr

    更新日期：1987-12-29 00:00:00

  • Interaction of tetrahydrofolate and other folate derivatives with bacterial sarcosine oxidase.

    abstract：:Sarcosine oxidase from Corynebacterium sp. P-1 binds 2 mol of tetrahydrofolate/mol of enzyme (KD = 8.8 microM). The same stoichiometry is observed with tetrahydropteroyltetraglutamate (KD = 15.4 microM). Binding is also observed with pteroyltetraglutamate and with 5-formyltetrahydrofolate. In the case of the pteroylmo...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi00397a029

    authors： Kvalnes-Krick K,Jorns MS

    更新日期：1987-11-17 00:00:00

  • Chemical modification of tryptophan residues in Escherichia coli succinyl-CoA synthetase. Effect on structure and enzyme activity.

    abstract：:Succinyl-CoA synthetase of Escherichia coli is an alpha 2 beta 2 protein containing active sites at the interfaces between alpha- and beta-subunits. The alpha-subunit contains a histidine residue that is phosphorylated during the reaction. The beta-subunit binds coenzyme A and probably succinate [see Nishimura, J. S. ...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi00370a061

    authors： Ybarra J,Prasad AR,Nishimura JS

    更新日期：1986-11-04 00:00:00

  • Determination of the rate and yield of B-side quinone reduction in Rhodobacter capsulatus reaction centers.

    abstract：:In the native purple bacterial reaction center (RC), light-driven charge separation utilizes only the A-side cofactors, with the symmetry related B-side inactive. The process is initiated by electron transfer from the excited primary donor (P*) to the A-side bacteriopheophytin (P* --> P+ H(A)-) in approximately 3 ps. ...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi060277x

    authors： Kee HL,Laible PD,Bautista JA,Hanson DK,Holten D,Kirmaier C

    更新日期：2006-06-13 00:00:00

  • Operative Binding of Class I Release Factors and YaeJ Stabilizes the Ribosome in the Nonrotated State.

    abstract：:During translation, the small subunit of the ribosome rotates with respect to the large subunit primarily between two states as mRNA is being translated into a protein. At the termination of bacterial translation, class I release factors (RFs) bind to a stop codon in the A-site and catalyze the release of the peptide ...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/acs.biochem.7b00824

    authors： Casy W,Prater AR,Cornish PV

    更新日期：2018-04-03 00:00:00

  • Detection of RNA-Protein Interactions in Living Cells with SHAPE.

    abstract：:SHAPE-MaP is unique among RNA structure probing strategies in that it both measures flexibility at single-nucleotide resolution and quantifies the uncertainties in these measurements. We report a straightforward analytical framework that incorporates these uncertainties to allow detection of RNA structural differences...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/acs.biochem.5b00977

    authors： Smola MJ,Calabrese JM,Weeks KM

    更新日期：2015-11-24 00:00:00

  • Inhibition of iodine-125-labeled human follitropin binding to testicular receptor by epidermal growth factor and synthetic peptides.

    abstract：:Two tetrapeptide sequence homologies between mouse epidermal growth factor precursor (mEGFP) and human follitropin (FSH) were revealed by a computer program that identifies identical residues among polypeptide sequences. The two tetrapeptides, Lys-Thr-Cys-Thr (KTCT) and Thr-Arg-Asp-Leu (TRDL), are present in the hormo...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi00357a053

    authors： Sluss PM,Krystek SR Jr,Andersen TT,Melson BE,Huston JS,Ridge R,Reichert LE Jr

    更新日期：1986-05-06 00:00:00

  • Nucleotide- and substrate-induced conformational transitions in the CBS domain-containing pyrophosphatase of Moorella thermoacetica.

    abstract：:In contrast to all other known pyrophosphatases, Moorella thermoacetica pyrophosphatase (mtCBS-PPase) contains nucleotide-binding CBS domains and is thus strongly regulated by adenine nucleotides. Stopped-flow measurements using a fluorescent AMP analogue, 2'(3')-O-(N-methylanthranoyl)-AMP (Mant-AMP), reveal that nucl...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi9019737

    authors： Jämsen J,Baykov AA,Lahti R

    更新日期：2010-02-09 00:00:00

  • Electrostatic effects in myoglobin. Application of the modified Tanford-Kirkwood theory to myoglobins from horse, California grey whale, harbor seal, and California sea lion.

    abstract：:The modified Tanford-Kirkwood electrostatic theory (Shire et al., 1974a) was applied to ferrimyoglobins from the following animal species: sperm whale (Physeter catodon), horse, California grey whale (Eschrichtius gibbosus), harbor seal (Phoca vitulina), and California sea lion (Zalophus californianus). Computations w...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi00678a002

    authors： Shire SJ,Hanania GI,Gurd FR

    更新日期：1975-04-08 00:00:00

  • Catalytic roles of the distal site asparagine-histidine couple in peroxidases.

    abstract：:There are highly conserved hydrogen bonds between the distal His and the adjacent Asn in many peroxidases. Although the crystal structure of horseradish peroxidase C (HRP) is not available, comparison of the amino acid sequence with cytochrome c peroxidase indicates that Asn70 is making the hydrogen bond with the dist...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi961740g

    authors： Nagano S,Tanaka M,Ishimori K,Watanabe Y,Morishima I

    更新日期：1996-11-12 00:00:00

  • Increased Turnover at Limiting O2 Concentrations by the Thr(387) → Ala Variant of HIF-Prolyl Hydroxylase PHD2.

    abstract：:PHD2 is a 2-oxoglutarate, non-heme Fe(2+)-dependent oxygenase that senses O2 levels in human cells by hydroxylating two prolyl residues in the oxygen-dependent degradation domain (ODD) of HIF1α. Identifying the active site contacts that determine the rate of reaction at limiting O2 concentrations is crucial for unders...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi501540c

    authors： Pektas S,Taabazuing CY,Knapp MJ

    更新日期：2015-05-12 00:00:00

  • Interaction of fusogenic synthetic peptide with phospholipid bilayers: orientation of the peptide alpha-helix and binding isotherm.

    abstract：:We studied the binding characteristics of a synthetic 20-residue peptide to supported single planar bilayers of phosphatidylcholine, and the orientation of the peptide by Fourier-transform infrared spectroscopy with an attenuated total reflection method. This peptide, designed to resemble a putative fusion peptide of ...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi952547+

    authors： Ishiguro R,Matsumoto M,Takahashi S

    更新日期：1996-04-16 00:00:00

  • Isolation of high-affinity peptide antagonists of 14-3-3 proteins by phage display.

    abstract：:The 14-3-3 proteins interact with diverse cellular molecules involved in various signal transduction pathways controlling cell proliferation, transformation, and apoptosis. To aid our investigation of the biological function of 14-3-3 proteins, we have set out to identify high-affinity antagonists. By screening phage ...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi991353h

    authors： Wang B,Yang H,Liu YC,Jelinek T,Zhang L,Ruoslahti E,Fu H

    更新日期：1999-09-21 00:00:00

  • Nuclear magnetic resonance solution structure of an undecanucleotide duplex with a complementary thymidine base opposite a 10R adduct derived from trans addition of a deoxyadenosine N6-amino group to (-)-(7R,8S,9R,10S)-7,8-dihydroxy- 9,10-epoxy-7,8,9,10-t

    abstract：:The solution structure of a modified undecamer duplex containing (-)-(7R,8S,9R,10S)-7,8-dihydroxy-9,10-epoxy-7,8,9,10-tetrahydrobenzo[a] pyrene covalently bonded through trans ring opening at C10 of the epoxide by the N6-amino group of deoxyadenosine (dA) was studied. This diol epoxide 1 diastereomer has the benzylic ...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi00028a009

    authors： Schurter EJ,Sayer JM,Oh-hara T,Yeh HJ,Yagi H,Luxon BA,Jerina DM,Gorenstein DG

    更新日期：1995-07-18 00:00:00

  • A Fold-Independent Interface Residue Is Crucial for Complex Formation and Allosteric Signaling in Class I Glutamine Amidotransferases.

    abstract：:The members of the glutamine amidotransferase (GATase) family catalyze the incorporation of ammonia within numerous metabolic pathways and can be categorized in two classes. Here, we concentrated on class I GATases, which are heteromeric enzyme complexes consisting of synthase subunits and glutaminase subunits with a ...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/acs.biochem.9b00286

    authors： Semmelmann F,Hupfeld E,Heizinger L,Merkl R,Sterner R

    更新日期：2019-06-04 00:00:00

  • Steric hindrance as a basis for structure-based design of selective inhibitors of protein-tyrosine phosphatases.

    abstract：:Utilizing structure-based design, we have previously demonstrated that it is possible to obtain selective inhibitors of protein-tyrosine phosphatase 1B (PTP1B). A basic nitrogen was introduced into a general PTP inhibitor to form a salt bridge to Asp48 in PTP1B and simultaneously cause repulsion in PTPs containing an ...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi011389l

    authors： Iversen LF,Andersen HS,Møller KB,Olsen OH,Peters GH,Branner S,Mortensen SB,Hansen TK,Lau J,Ge Y,Holsworth DD,Newman MJ,Hundahl Møller NP

    更新日期：2001-12-11 00:00:00

  • Three-dimensional structure of acyl carrier protein determined by NMR pseudoenergy and distance geometry calculations.

    abstract：:Distance constraints from two-dimensional NMR cross-relaxation data are used to derive a three-dimensional structure for acyl carrier protein from Escherichia coli. Several approaches to structure determination are explored. The most successful proves to be an approach that combines the early stages of a distance geom...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi00416a046

    authors： Holak TA,Kearsley SK,Kim Y,Prestegard JH

    更新日期：1988-08-09 00:00:00

  • The Non-native Helical Intermediate State May Accumulate at Low pH in the Folding and Aggregation Landscape of the Intestinal Fatty Acid Binding Protein.

    abstract：:There has been widespread interest in studying early intermediate states and their roles in protein folding. The interest in intermediate states has been further emphasized in the recent literature because of their implications for protein aggregation. Unfortunately, direct kinetic characterization of intermediates ha...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/acs.biochem.6b00390

    authors： Sarkar-Banerjee S,Chowdhury S,Paul SS,Dutta D,Ghosh A,Chattopadhyay K

    更新日期：2016-08-16 00:00:00

  • Biochemical and Structural Analysis of FomD That Catalyzes the Hydrolysis of Cytidylyl ( S)-2-Hydroxypropylphosphonate in Fosfomycin Biosynthesis.

    abstract：:In fosfomycin biosynthesis, the hydrolysis of cytidylyl ( S)-2-hydroxypropylphosphonate [( S)-HPP-CMP] to afford ( S)-HPP is the only uncharacterized step. Because FomD is an uncharacterized protein with a DUF402 domain that is encoded in the fosfomycin biosynthetic gene cluster, FomD was hypothesized to be responsibl...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/acs.biochem.8b00690

    authors： Sato S,Miyanaga A,Kim SY,Kuzuyama T,Kudo F,Eguchi T

    更新日期：2018-08-14 00:00:00

  • Insertion and orientation of a synthetic peptide representing the C-terminus of the A1 domain of Shiga toxin into phospholipid membranes.

    abstract：:Shiga toxin is a bacterial protein composed of one A and five B subunits. Its A chain possesses a protease sensitive loop (Cys-242-Cys-261) that is cleaved to produce an enzymatically active A1 domain and an A2 fragment associated with its B subunit pentamer. The proposed mode of action of the toxin is linked to its r...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi960177z

    authors： Saleh MT,Ferguson J,Boggs JM,Gariépy J

    更新日期：1996-07-23 00:00:00

  • Structural composition of canine secretory component and immunoglobulin A.

    abstract：:Dog serum and colostral immunoglobulin A (IgA) and free secretory component from colostrum were isolated using affinity chromatography. Both serum and colostral IgA showed similar susceptibility to reduction with dithiothreitol, but only colostral IgA released the additional subunit, bound secretory component. This re...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi00684a010

    authors： Thompson RE,Reynolds HY,Waxdal MJ

    更新日期：1975-07-01 00:00:00

  • Protein which interacts with a stimulatory factor of RNA polymerase II of Ehrlich ascites tumor cells.

    abstract：:When partially purified Ehrlich ascites tumor RNA polymerase II was further purified on a column of phosphocellulose, stimulation of its catalysis of RNA synthesis by stimulatory factor S-II was greatly decreased. This decrease in sensitivity to the stimulatory factor was reversible: the enzyme eluted from phosphocell...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi00645a006

    authors： Kuroiwa A,Mizuno D,Natori S

    更新日期：1977-12-27 00:00:00

  • Cardiac-specific Nkx2.5 homeodomain: conformational stability and specific DNA binding of Nkx2.5(C56S).

    abstract：:The cardiac-specific Nkx2.5 homeodomain has been expressed as a 79-residue protein with the oxidizable Cys(56) replaced with Ser. The Nkx2.5 or Nkx2.5(C56S) homeodomain is 73% identical in sequence to and has the same NMR structure as the vnd (ventral nervous system defective)/NK-2 homeodomain of Drosophila when bound...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi050835s

    authors： Fodor E,Mack JW,Maeng JS,Ju JH,Lee HS,Gruschus JM,Ferretti JA,Ginsburg A

    更新日期：2005-09-20 00:00:00

  • A cysteine-rich CCG domain contains a novel [4Fe-4S] cluster binding motif as deduced from studies with subunit B of heterodisulfide reductase from Methanothermobacter marburgensis.

    abstract：:Heterodisulfide reductase (HDR) of methanogenic archaea with its active-site [4Fe-4S] cluster catalyzes the reversible reduction of the heterodisulfide (CoM-S-S-CoB) of the methanogenic coenzyme M (CoM-SH) and coenzyme B (CoB-SH). CoM-HDR, a mechanistic-based paramagnetic intermediate generated upon half-reaction of t...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi700679u

    authors： Hamann N,Mander GJ,Shokes JE,Scott RA,Bennati M,Hedderich R

    更新日期：2007-11-06 00:00:00

  • Uracil DNA-glycosylase/glyceraldehyde-3-phosphate dehydrogenase is an Ap4A binding protein.

    abstract：:A 37 kDa protein that binds to diadenosine tetraphosphate (Ap4A) was purified from human HeLa cells and identified as uracil DNA glycosylase/glyceraldehyde-3-phosphate dehydrogenase (UDG/GAPDH). Utilizing photoaffinity labeling with [alpha-32P]8N3-Ap4A, an Ap4A binding protein of 37 kDa was identified from HeLa cell n...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi00030a007

    authors： Baxi MD,Vishwanatha JK

    更新日期：1995-08-01 00:00:00

  • Nematode Sgt1-homologue D1054.3 binds open and closed conformations of Hsp90 via distinct binding sites.

    abstract：:Heat shock protein 90 (Hsp90) is a highly conserved ATP-driven machine involved in client protein maturation, folding, and activation. The chaperone is supported by a set of cochaperones that confer client specificities. One of those proteins is the suppressor of G2 allele of skp1 (Sgt1), which participates together w...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi5000542

    authors： Eckl JM,Drazic A,Rutz DA,Richter K

    更新日期：2014-04-22 00:00:00

  • Aggregation studies on fluorescein-coupled cobra venom phospholipase A2.

    abstract：:Phospholipase A2 from Naja naja naja venom (Indian cobra) undergoes a concentration-dependent aggregation, and at an assay concentration of 1 microgram mL-1, it exists as a monomer. However, there is some evidence that the enzyme is actually active as a dimer or higher order aggregate. Previous attempts to determine t...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi00343a018

    authors： Hazlett TL,Dennis EA

    更新日期：1985-10-22 00:00:00

  • Mutagenesis of a conserved glutamate reveals the contribution of electrostatic energy to adenosylcobalamin co-C bond homolysis in ornithine 4,5-aminomutase and methylmalonyl-CoA mutase.

    abstract：:Binding of substrate to ornithine 4,5-aminomutase (OAM) and methylmalonyl-CoA mutase (MCM) leads to the formation of an electrostatic interaction between a conserved glutamate side chain and the adenosyl ribose of the adenosylcobalamin (AdoCbl) cofactor. The contribution of this residue (Glu338 in OAM from Clostridium...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi3012719

    authors： Makins C,Pickering AV,Mariani C,Wolthers KR

    更新日期：2013-02-05 00:00:00

  • Raman spectroscopic studies of NAD coenzymes bound to malate dehydrogenases by difference techniques.

    abstract：:We report here on the Raman spectra of NADH, 3-acetylpyridine adenine dinucleotide, APAD+, and a fragment of these molecules, adenosine 5'-diphosphate ribose (ADPR) bound to the mitochondrial (mMDH) and cytoplasmic (or soluble, sMDH) forms of malate dehydrogenase. We observe changes in the Raman spectrum of the adenos...

    journal_title：Biochemistry

    pub_type： 杂志文章

    doi：10.1021/bi00100a011

    authors： Deng H,Burgner J,Callender R

    更新日期：1991-09-10 00:00:00