Posts Tagged ‘waterproof cover for bag’

Topalovića Glavica

onsdag, september 13th, 2017

Topalovića Glavica är ett berg i Bosnien och Hercegovina. Det ligger i entiteten Republika Srpska, i den centrala delen av landet, 120 km nordväst om huvudstaden Sarajevo. Toppen på Topalovića Glavica är 579 meter över havet, eller 93 meter över den omgivande terrängen. Bredden vid basen är 1,4 km.

Terrängen runt Topalovića Glavica är kuperad. Den högsta punkten i närheten är Marjanovo Gnijezdo, 837 meter över havet, 4,4 km öster om Topalovića Glavica. Närmaste större samhälle är Kotor-Varoš, 4,7 km söder om Topalovića Glavica. I trakten runt Topalovića Glavica finns ovanligt många namngivna klippformationer.

I omgivningarna runt Topalovića Glavica växer i huvudsak lövfällande lövskog. Runt Topalovića Glavica är det ganska tätbefolkat, med 67 invånare per kvadratkilometer

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. Trakten ingår i den hemiboreala klimatzonen. Årsmedeltemperaturen i trakten är 11 °C. Den varmaste månaden är juli, då medeltemperaturen är 22&nbsp waterproof cover for bag;°C, och den kallaste är januari, med -2 °C. Genomsnittlig årsnederbörd är 1 472 millimeter. Den regnigaste månaden är maj, med i genomsnitt 197 mm nederbörd, och den torraste är mars personalized stainless steel water bottles, med 86 mm nederbörd.

Juvenile hormone diol kinase

lördag, mars 25th, 2017

The conjugate (10S,11S) JH diol phosphate is the product of a two-step enzymatic process: conversion of JH to JH diol and then addition of a phosphate group to C10. The enzyme responsible for the phosphorylation of JH diol is JH diol kinase (JHDK), which was first characterized from the Malpighian tubules of early fifth instars of M. sexta. JHDK (EC was discovered when an analysis of JH I metabolites in vivo yielded, in addition to the expected metabolites, a very polar JH I conjugate that was subsequently identified as JH I diol phosphate. Maxwell et al. showed JHDK to contain 3 potential calcium binding sites, and a single ATP-Mg2+ binding site (p-loop). The modeled structure contains nine helices, one beta sheet, and 10 loops. JHDK is also present in the silkworm, where it also functions as homodimer. It lacks a JH response element; Li et al. (2005). It has a high degree of identity to M. sexta JHDK. Later Uno et al. (2007) characterized the A. mellifera enzyme in a proteomic study. It has 183 amino acid residues water bottle metal. More recently, Zeng et al. (2015) have characterized JHDK from Spodoptera litura. It also has 183 amino acid residues, just as does the B. mori enzyme. These enzymes all have high sequence similarity. The M. sexta enzyme contains 184 residues.

JHDK from M. sexta Malpighian tubules is a cytosolic protein composed of two identical subunits of 20 kDa, as determined by MS. Gel filtration studies indicate it has a molecular mass of approximately 43 kDa. JHDK displays a Km in the nanomolar range for JH I diol, which is appropriate for an enzyme responsible for clearance of a hormone whose titers rarely exceeds 10 nM. Most significantly waterproof cover for bag, the catalytic activity of JHDK parallels developmentally that of JHEH, a requisite if JH diol phosphate is a legitimate terminal metabolite. Analysis of the kcat/Km ratio for the diols of JH I, II, and III indicates that JH I diol is the preferred substrate, suggesting a preference for an ethyl group at the C7 position. JHDK requires both Mg2+ and ATP for activity. Characterization of the juvenile hormone epoxide hydrolase (JHEH) and juvenile hormone diol phosphotransferase (JHDPT) from Manduca sexta Malpighian tubules. Arch. Insect Biochem. Physiol. 30, 255-270 ), although excess Mg2+ and Ca2+ inhibit its activity.

The specificity of JHDK for JH I diol is relatively high, considering the multitude of potential phosphate acceptor groups present in a cell. The enzyme does not recognize methyl geranoate diol (one isoprenyl unit shorter than JH) nor methyl geranylgeranoate diol (one isoprenyl group longer than JH), yet it does recognize JH I ethyl ester diol. It also recognizes both JH diol enantiomers, indicating that the absolute stereospecificity of the hydroxy groups is of minor importance. Most surprising is the enzyme’s inability to recognize JH acid diols. Because JH acid diol cannot be phosphorylated by JHDK, the generally accepted pathway for JH catabolism (JH acid is converted to JH acid diol) must be reconsidered. Still, the role of cellular JHE becomes problematic if the pathway catalyzed by JHEH and JHDK is the major pathway for JH catabolism in the cell. The fact that JH diol phosphate is a significant metabolite certainly weakens the long-held dogma about JH catabolism. While JHE has been noted to have phosphatase activity, to our knowledge it has never been tested on JHDK.

The sequence and hypothetical structures of M. sexta, D. melanogaster, and B. mori JHDK have been analyzed. A partial characterization of JHDK from whole-body homogenates of D. melanogaster indicates that it is similar to the enzyme in M. sexta, with the exception of its subunit structure. The active D. melanogaster JHDK is a monomer of ~20 kDa, while the active M. sexta (GenBank accession number: AJ430670) and B. mori JHDKs (GenBank accession number: AY363308) are composed of two identical 20 kDa subunits. Similarities in chromatographic properties, isoelectric point, and enzyme activity led to conclude that sarcoplasmic calcium-binding protein 2 (dSCP2) is the probable D. melanogaster homologue of M. sexta JHDK. The M. sexta gene codes for an enzyme that has 59% sequence identity and >80% similarity to dSCP2 of D. melanogaster (GenBank accession number: AF093240; CG14904). Li et al. reported that the B. mori JHDK is composed of a single exon of 637 bp. The B. mori JHDK is expressed most prevalently in the gut, as determined by Northern blot analyses, and is not under the direct control of JH at the transcriptional level. Maxwell et al. generated a 3D model that they used for in silico docking simulations. They capitalized on the facts that the catalytic site of JHDK must contain a purine (GTP) binding site and hydrophobic pocket for JH diol, and that the scaffolding for dSCP2 is known. Surrounding the putative substrate-binding site, both the M. sexta and D. melanogaster JHDKs contain the three conserved nucleotide-binding elements common to nucleotide binding proteins. The model further demonstrates that the protein contains four domains that form two pairs of a helix-loop-helix motif (EF-hand;. Charge interactions in the hydrophobic binding pocket, as well as its depth (19 Â), are complementary to the extended conformation of the diol. Moreover, the hydrophobic nature of the binding pocket complements the C1 ester of the substrate and supports the observation that JH diol is the only substrate for this enzyme.

Abraham Hondius

torsdag, november 24th, 2016

Abraham Hondius, Extrait de La vie des peintres flamands, allemands et hollandois, avec des portraits gravés en taille-douce, une indication de leurs principaux ouvrages, & des réflexions sur leur différentes manières de Jean-Baptiste Descamps, Tome 3, p buy cheap football shirts online. 280

Abraham Hondius ou Abraham Danielsz. Hondius ou Abraham de Hondt (vers 1631 vacuum meat tenderizer, Rotterdam – , Londres) est un peintre néerlandais du siècle d’or. Il est connu pour ses peintures de paysages, de scènes de chasse, de scènes de genre militaire, de scènes religieuses et de portraits waterproof cover for bag.

Abraham Hondius est né vers 1631 à Rotterdam aux Pays-Bas.

Il est le fils d’un tailleur de pierre, Daniel Abramsz. de Hondt. Il étudie la peinture auprès des peintres Pieter de Bloot et Cornelis Saftleven. En 1659, il part s’installer à Amsterdam. En 1666, il quitte les Pays-Bas et se fixe définitivement à Londres.

Il meurt en 1691 à Londres et est enterré dans l’église St Bride dans la rue londonienne exercises for soccer goalies, Fleet Street.

La chasse au cerf,

Mercuris et Argos par Abraham Hondius

L’Annonce aux bergers

Sur les autres projets Wikimedia :

Bert Tann

lördag, november 5th, 2016

* Senior club appearances and goals counted for the domestic league only.

Bert Tann (4 May 1914 – 12 May 1972) was a football manager and player, who managed Bristol Rovers for 18 years, from 1950 to 1968. He was the longest-serving post-war manager of Rovers, and the second longest overall behind Alfred Homer.

During his playing career in the 1930s he was primarily a wing-half kids footy socks, and after brief spells with Clapton Orient and Romford he joined Charlton Athletic. He first played a league game for Charlton in the 1933–34 season, and went on to play in 19 league games for them until 1938–39. During World War II, he guested for Southampton, making 36 appearances. He also appeared as a guest player for West Ham United in World War II making just one appearance.

In 1947 he became coach of Fredrikstad in Norway safe plastic water bottles. He led them to the 1946/47 Ostfoldserien championship waterproof cover for bag.

In 1950 he became manager of Bristol Rovers, and with Tann in charge, Rovers were promoted to the Football League Second Division for the first time in 1952-53, and he led them to 6th-place finishes in both 1955-56 and 1958-59, as well to the quarter-finals of the FA Cup in 1950-51 and 1957-58 where to get football jerseys.

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