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Myoglobin molecular weight

Myoglobin je globulární protein tvořený jediným řetězcem aminokyselin, který obsahuje jako prostetickou složku hem.Reverzibilně váže a přenáší kyslík ve svalových buňkách. Myoglobin z kosterního svalstva i myokardu je identický.V ledvinách je filtrován glomerulární membránou a vylučován do moči. Má velmi krátký biologický poločas - 10-20 minut Property Name Property Value Reference; Molecular Weight: 1218.4 g/mol: Computed by PubChem 2.1 (PubChem release 2019.06.18) XLogP3-AA-5.8: Computed by XLogP3 3.0 (PubChem release 2019.06.18 The molecular weight of Myoglobin is 16,700, which is a compact macromolecule with oblate, spheroid shaped macromolecule. The overall molecular dimensions are 45 X 35 X 25 Ao. It contains a heme (prosthetic) responsible for its main function (carrying of oxygen molecules to muscle tissues) and Globin protein Entry name i: MYG_HUMAN: Accession i: P02144 Primary (citable) accession number: P02144 Secondary accession number(s): Q52H51, Q5THY7: Entry history i: Integrated into UniProtKB/Swiss-Prot: : July 21, 1986: Last sequence update: : January 23, 2007: Last modified: : December 2, 2020: This is version 193 of the entry and version 2 of the sequence. See complete history.: Entry status i: Reviewed. Myoglobin is a low-molecular weight protein of 16,000 Da that contains one heme and binds one molecule of O 2 per molecule of protein. Tissue content of myoglobin depends on the tissue and the species. Highly oxidative muscle fibers contain a lot of myoglobin

The correct molecular weight of myoglobin, a common calibrant for mass spectrometry. Rapid Commun Mass Spectrom. 1992 Jan;6(1):32-6. Our vendor of choice for this standard is Sigma-Aldrich 60 nmol vials of horse myoglobin Sigma-Aldrich product number A8673-1VL and A8673-5X1VL Thus, the correct molecular weight of horse myoglobinis 16951.49 and that of the sperm whale protein is 17199.91 Myoglobin has been obtained in pure crystalline form from many sources. It has a molecular weight of 16,700, about one-fourth that of hemoglobin. Though the heme portion of all myoglobins is the same, the protein portions vary considerably between species. Get exclusive access to content from our 1768 First Edition with your subscription

Myoglobin - WikiSkript

Myoglobin(42-50)[sperm whale] C58H91N17O12 - PubChe

  1. Myoglobin is an iron- and oxygen-binding protein found in the muscle tissue of vertebrates in general and in almost all mammals. It is related to hemoglobin, which is the iron- and oxygen-binding protein in blood, specifically in the red blood cells. It has a molecular weight of 17,699 (with heme)daltons, and is the primary oxygen-carrying.
  2. antly in striated muscle tissue (skeletal and cardiac muscle). Myoglobin is liberated from damaged heart muscle cells such as occurs during acute myocardial infarction
Proteins simplified

Myoglobin. Gene. MB. Organism. Bos taurus (Bovine) Status. Reviewed-Annotation score: -Experimental Main funding by: National Institutes of Health The European Molecular Biology Laboratory State Secretariat for Education, Research and Innovation SERI Myoglobin from equine skeletal muscle, 95-100%, essentially salt-free, lyophilized powder, M5696 Myoglobin from equine skeletal muscle, BioUltra, ≥98% (SDS-PAGE) Haemoglobin has 64 kDa molecular weight whereas myoglobin has a molecular weight of 16.7 kDa. Haemoglobin has a low affinity to bind with oxygen while myoglobin has a high affinity to bind with oxygen Predicted General Properties of the Myoglobin Protein (Homo sapiens) - Primary Sequence Analysis (with ProtParam) b. Number of amino acids: 154 . Molecular weight: 17183.8 . Theoretical pI: 7.14 . Total number of negatively charged residues (Asp + Glu): 22 . Total number of positively charged residues (Arg + Lys): 2 Thus, the correct molecular weight of horse myoglobin is 16,951.49 and that of the sperm whale protein is 17,199.91. Myoglobins from horse heart muscle, horse skeletal muscle and sperm whale are widely used as calibration standards or test compounds for various mass spectrometric methodologies. In all such cases reported in the literature, a.

What is Myoglobin? What is the function of Myoglobin

Native Human Myoglobin is a heme containing oxygen carrier that stores oxygen in muscles. It consists of a single polypeptide chain with a molecular weight of ~16 kDa. Sequence analysis shows that it is structurally related to haemoglobin Myoglobin is a cytoplasmic hemoprotein, expressed solely in cardiac myocytes and oxidative skeletal muscle fibers, that reversibly binds O2 by its heme residue, a porphyrin ring:iron ion complex. Since the initial discovery of its structure over 40 years ago, wide-ranging work by many investigators has added importantly to our understanding of its function and regulation Myoglobin is a heme protein found in skeletal and cardiac muscle that has attracted considerable interest as an early marker of MI. Its low molecular weight accounts for its early release profile.

MB - Myoglobin - Homo sapiens (Human) - MB gene & protei

Students determine the molecular weight of Mb in their mixtures and compare it to the literature value (17.6 kDa for Sigma M‐0630); they also determine the percentage of Mb in each mixture (20 ± 3%), showing that the desalting Sephadex G‐25 column merely serves to remove the excess ferricyanide, but does not appreciably separate any of the. Native Human Myoglobin protein is a Native Full length protein 2 to 154 aa range, >=96% purity and validated in ID, SDS-PAGE. Some batches were tested by size exclusion HPLC and a single peak of the expected molecular weight could be observed. Read More. Abcam Scientific Support. Answered on May 10 201

presence of the myoglobin aggregate could be demonstrated by gel filtration on Sephadex G-1 00 Superfine, which also provided a means of isolating it. Gel filtration on Sephadex Q-100 showed the molecular weights of the equine and bovine nioyglobin aggregates to be about 35000 an Myoglobin is a relatively small protein that contains a heme group with an iron atom, and whose function is to store and transport oxygen. Structure: Myoglobin is a globular protein consisting of a single chain of approximately one hundred and fifty amino acids. Additionally, its molecular weight is approximately 18 Kd Property Name Property Value Reference; Molecular Weight: 1455.6 g/mol: Computed by PubChem 2.1 (PubChem release 2019.06.18) XLogP3-AA-9.3: Computed by XLogP3 3.0 (PubChem release 2019.06.18 Myoglobin was the first protein to have its atomic structure determined, revealing how it stores oxygen in muscle cells. R. E. Hubbard & A. J. Wilkinson (1990) Determination of the crystal structure of recombinant pig myoglobin by molecular replacement and its refinement. Acta Crystallographica B, 46, 370-377

Video: Myoglobin - an overview ScienceDirect Topic

DOI: 10.1002/RCM.1290060108 Corpus ID: 23635667. The correct molecular weight of myoglobin, a common calibrant for mass spectrometry. @article{Zaia1992TheCM, title={The correct molecular weight of myoglobin, a common calibrant for mass spectrometry.}, author={J. Zaia and R. Annan and K. Biemann}, journal={Rapid communications in mass spectrometry : RCM}, year={1992}, volume={6 1}, pages={ 32-6 } only one peak indicated that either Substance A was of similar molecular weight (assuming similar molecular shape) or that an association complex was formed with the myoglobin which prevented resolution. This prob- lem has not been resolved, but some interesting data on protein associatio

Myoglobin 16951.26 100 16951.2703 1. 10 pmol Myoglobin_TFA_P1-E-7_01_12768.d: +MS, 11.2-11.4min, -Peak Bkgrnd, Smoothed (0.20,3,SG), Baseline subtracted(0.80), Deconvoluted (MaxEnt, 823.57-2444.28, *4.27083, 3000) 0 2 4 6 8 x106 Intens. 20000 40000 60000 80000 100000 120000 140000 160000 180000 m/z 16951.260 The molecular weight of sperm whale myoglobin is 17.8 kDa. The myoglobin content of sperm whale muscle is about 80.0 g • kg-1. In contrast, the myoglobin content of some human muscles is about 8.00 g • kg-1 The molecular weight of sperm whale myoglobin is 17.8 kDa. The myoglobin content of sperm whale muscle is about 80.0 g - kg. In contrast, the myoglobin content of some human muscles is about 8.00 g. kg. Compare the amounts of O, bound to myoglobin in human muscle and in sperm whale muscle To the Editor: Bosch and colleagues (July 2 issue) 1 observe that although conventional hemodialysis filters do not remove myoglobin (molecular weight, 17.8 kD), hemodiafiltration with..

Horse Myoglobin - Ion Sourc

  1. Myoglobin has been obtained in pure crystalline form from many sources. It has a molecular weight of 16,700, which is about a quarter that of hemoglobin. Though the heme portion of all myoglobins is the same, the protein portions vary considerably between species
  2. o acids, containing a heme (iron-containing porphyrin) prosthetic group in the center around which the remaining apoprotein folds
  3. Osteocalcin is a protein with a molecular mass of 5,800 daltons, and myoglobin is a large molecule with a molecular mass of 17,200 daltons
  4. M is the molecular weight standard (Pharmacia). Human myoglobin kDa 94 67 43 30 20 14.4 M µg 3 6 µg Human myoglobin Myoglobin is purified from human cardiac tissue by several chromatographic steps including gel-filtration and anion-exchange chromatography. After SDS-PAGE in reducing conditions myoglobin is presented by a single band with.
  5. o acids, joined via peptide bonds
  6. o acids, containing a heme (iron-containing porphyrin) prosthetic group in the center around which the remaining apoprotein folds. With a molecular weight of 16.7 kDa, it is the primary oxygen-carrying pigment of muscle tissues

Immunoglobulin: approximate MW/ kDa (g·mol −1)number of subunits: pI: A280. Mg/ml) IgA, human: 162: 4 n.a. 1.34: IgE, human: 190: 4 n.a. 1.53: IgG, goat: 144: 4 n. myoglobin: [ mi´o-glo″bin ] the oxygen-transporting pigment of muscle, a type of hemoprotein resembling a single subunit of hemoglobin , being composed of one globin polypeptide chain and one heme group

The correct molecular weight of myoglobin, a common

Experimental Molecular Weight of Myoglobin Literature Molecular Weight of Myoglobin 16, 982 Da 16, 951.49 1 Da Table 2 above displays the differences in molecular weight between the literature and experimental values of the molecular weight of myoglobin. Calculations: Calculation of the molecular weight of myoglobin Linear regression: y =− 0. of low molecular weight, easily pre? pared in quantity, readily crystallized, and not already being studied by x-ray methods elsewhere. Myoglobin seemed to satisfy these criteria, and it had the additional advantage of being closely related to hemoglobin, which had been the object of Perutz's attention for many years, and of sharing with hemo Boulton FE, Huntsman RG, Romero Herrera A, Lorkin PA, Lehmann H: The third variant of human myoglobin showing an unusual amino acid substitution: 138(H16)arginine--tryptophan. Biochim Biophys Acta. 1971 Mar 23;229(3):716-9 The molecular weight of myoglobin is 17,000. The spatial structure of myoglobin resembles the beta chain of hemoglobin. Myoglobin combines reversibly with oxygen even at low partial pressures of oxygen. This is of great physiological importance: the partial pressure of oxygen decreases sharply during muscle contraction as a result of.

The concentration of myoglobin was measured spectrophoto- metrically. The extinction coefficient (E&zEs,liter) of human myoglobin was determined for several preparations from simul- taneous dry-weight determinations at 105 and spectrophoto- metric analysis at 280 rnp. For a molecular weight of 17,500 Purified human myoglobin - liquid Preparation Purified myoglobulin from human heart Buffer Solution Phosphate buffered saline Preservative Stabilisers. 0.09%: Sodium Azide (NaN 3) Purity >96% by SDS PAGE Approx. Protein Concentrations 1.0 mg/ml Protein Molecular Weight 17.5 kDa. Storage Information. Storage Store at +4 o C. DO NOT FREEZE. This. Myoglobin definition, hemoglobin of muscle, weighing less and carrying more oxygen and less carbon monoxide than blood hemoglobin. See more Myoglobin Human Recombinant Protein Myoglobin Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 17.67 kDa. The Myoglobin is purified by proprietary chromatographic techniques. SKU: PROTP02144-1 PROTP0 Myoglobin (Mb) stores dioxygen in muscles, and is a fundamental model protein widely used in molecular design. The presence of dimeric Mb has been known for more than forty years, but its structural and oxygen binding properties remain unknown

Myoglobin protein Britannic

  1. o acids and a molecular weight of 17.7 kDa 1, 2, 4. It is structurally similar to hemoglobin, which is the iron- and oxygen binding protein in blood
  2. All lanes : Anti-Myoglobin antibody [EP3081Y] (ab77232) at 1/5000 dilution (Purified) Lane 1 : Human muscle lysate with 5% NFDM/TBST Lane 2 : Mouse muscle lysate with 5% NFDM/TBST Lane 3 : Rat muscle lysate with 5% NFDM/TBST Lysates/proteins at 20 µg per lane. Secondary All lanes : Goat Anti-Rabbit IgG H&L (HRP) at 1/20000 dilution (Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated
  3. Source: Bovine Erythrocytes Hemoglobin is the major component of mammalian erythrocytes where it functions as the oxygen-carbon dioxide transport system. The molecule is composed of a heme group with four peptide chains and has a molecular weight of 64.5 kDa
  4. Mouse monoclonal Myoglobin antibody [6H8B5]. Validated in WB, IHC and tested in Human. Cited in 1 publication(s). Independently reviewed in 1 review(s). Immunogen corresponding to recombinant ful
  5. Myoglobin has 8 alpha helices and a hydrophobic core. Myoglobins molecular weight is 16.7 kDa, and it is the primary oxygen-carrying pigment of muscle tissues. The binding of oxygen in myoglobin is different from the cooperative oxygen binding in hemoglobin, since positive collaboration is a property of multimeric/oligomeric proteins only

Determination of myoglobin, a low molecular weight haeme protein (17.8 kDa), present in both cardiac and skeletal muscle, is an old test with new perspectives. Advantages and disadvantages of myoglobin determination are well known; recent availability of rapid and accurate methods for the assay of t Hemoglobin A (the type most often found in adults) has a molecular weight of 68 000 Da. Daltons (Da), atomic mass units (amu), and molar weight are all equivalent, so hemoglobin A has a molecular.

Myoglobin Protein Human PVALB MB Antigen ProSpe

Myoglobin has 8 alpha helices and a hydrophobic core. Myoglobinбпs molecular weight is 16.7 kDa, and it is the primary oxygen-carrying pigment of muscle tissues. The binding of oxygen in myoglobin is different from the cooperative oxygen binding in hemoglobin, since positive collaboration is a property of multimeric/oligomeric proteins only Buy Human Myoglobin protein from Cusabio. It is a Full length protein native protein produced in Purified from Human heart tissue and has been validated in ELISA, WB, SDS-PAGE. Latex enhanced turbidimetric immunoassay (LETIA), immunogen and other possible

iron metabolismMyoglobin test kit-Cardiovascular diseases-Bioda

Myoglobin >= 90 % SDS-PAGE, essentially salt-free

  1. Myoglobin is the sarcoplasmic heme protein primarily responsible for the meat color, and the chemistry of myoglobin is species specific. The mechanistic interactions between myoglobin and multiple extrinsic and intrinsic factors govern the color of raw as well as cooked meats
  2. (egg) 45 000 Albu
  3. ed in a Hilger `Uvispek' spectrophotometer each gave an absorption spectrum typical of carbon monoxide myoglobin. The molecular weight of the main component was deter
  4. Genetic Control of the Immune Response to Myoglobin. VII. Antibody Responses to Myoglobin Variants Reveal that Gene Restriction of the Antibody Responses to Myoglobin Antigenic Sites is Dependent on the Chemical Properties of the Sites. Immunological Communications, 10(6), 483-498. Imai, K. (2002). Myoglobin. Encyclopedia of Molecular Biology
  5. ed for all PEG network compositions. The diffusion coefficient depended on PEG molecular weight and initial solid content, with the slowest diffusion occurring through lower molecular weight, high-solid-content networks (D(gel) = 0.16 ± 0.02 × 10(-8) cm(2.
  6. Molecular mass of Myoglobin. Value. 17800 Dalton Range: Table - linkDalton. Organism. Sperm whale Physeter macrocephalus. Reference. Squire PG, Himmel ME. Hydrodynamics and protein hydration

Molecular weight of Myoglobin. A newer BioNumber version exists. click here. Value: 17800 Dalton Organism: Sperm whale Physeter macrocephalus Molecular mass of Bence Jones protein REI. Human Homo sapiens ID: 100397 Molecular mass of Malate dehydrogenase. Pig Sus species ID. Myoglobin has 8 alpha helices and a hydrophobic core. Myoglobin's molecular weight is 16.7 kDa, and it is the primary oxygen-carrying pigment of muscle tissues. The binding of oxygen in myoglobin is different from the cooperative oxygen binding in hemoglobin, since positive collaboration is a property of multimeric/oligomeric proteins only

Myoglobin is found in Type I, Type II A and Type II B muscle; however several studies indicate myoglobinis not found in smooth muscle. Recombinant Human Myoglobin produced in E. coli cells is a single non-glycosylated polypeptide chain containing 166 amino acids. rhMyoglobin has a molecular mass of 18.7 kDa analyzed by reducing SDS-PAGE and is. 1st. protein whose molecular weight was determined; 1st protein to be assigned a specific function - dioxygen transport; has a prosthetic group (non-amino acid) heme group (protoporphyrin IX with a ferrous ion) covalently attached to the protein. The heme group binds dioxygen Molecular Distillation Useful Vacuity. The Journal of Physical Chemistry B. Aqueous Solvation Free Energies of Ions and Ion−Water Clusters Based on an Accurate Value for the Absolute Aqueous Solvation Free Energy of the Proton. Nano Letters. Unusual Suppression of the Superconducting Energy Gap and Critical Temperature in Atomically Thin NbSe

Myoglobin - Worthington Enzyme Manua

Myoglobin Molecule -- Example of an Alpha Heli

  1. Myoglobin Myoglobin Model of helical domains in myoglobin.[1] Available structures: 1m6c, 1m6m, 1mdn, 1mnh, 1mni, 1mnj, 1mnk, 1mno, 1mwc, 1mwd, 1myg, 1myh
  2. imum molecular weight of hemoglobin was about 16,000, but there was little agreement about what multiple of 16,000 was..
  3. o acids can contribute significantly to the stability of proteins. To investigate the importance of the hydrophobic packing interface between helices G and H in the proximal heme pocket of horse heart myoglobin, the highly conserved a
  4. Myoglobin (molecular weight 17.8 kDa) asses the filter whereas the larger hemoglobin (molecular weight 68 kDa) is retained on filter. The filtrate was then tested for myoglobin with hemoglobin dipstick. Positive results were reported as myoglobin detected. The absence of red cells on microscopy confirmed that the discolored urine is caused by.
  5. Myoglobin and the structure of proteins Nobel Lecture, December 11, 1962 of low molecular weight, easily prepared in quantity, readily crystallized, MYOGLOBIN AND THE STRUCTURE OF PROTEINS 677 and not already being studied by X-ray methods elsewhere. Myoglobin seemed to satisfy these criteria, and had the additional advantages of being.

Myoglobin conversion to nmol/L, ng/mL, ng/dL, ng/100mL, ng

Myoglobin Protein Human Recombinant MB Antigen ProSpe

MB - Myoglobin - Bos taurus (Bovine) - MB gene & protei

A polymer sorbent clears myoglobin from blood and/or other physiological fluids and solutions. Normal saline or human serum in which myoglobin was dissolved is perfused by a peristaltic pump through a column packed with the polymer sorbent. After a four-hour perfusion, the myoglobin level in normal saline fell from initial levels to virtually undetectable levels Myoglobin is a heme-protein normally found in skeletal and cardiac muscle with a molecular weight of 17.8 kDa. It constitutes about 2 percent of total muscle protein and is responsible for transporting oxygen within muscle cells. When muscle cells are damaged, Myoglobin is released into the blood rapidly due to its relatively small size Myoglobin General: Myoglobin is a single-chain globular protein of 153 amino acids, containing a heme (iron-containing porphyrin) prosthetic group in the center around which the remaining apoprotein folds. It has eight alpha helices and a hydrophobic core (porphyrin ring). It has a molecular weight o Osteocalcin is a protein with a molecular mass of 5,800 daltons, and myoglobin is a large molecule with a molecular mass of 17,200 daltons. The aim of this study was to evaluate the impact of OL-HDF on in vivo removal of a wide spectrum of solutes (urea, creatinine, osteocalcin, β2-microglobulin, and myoglobin) in comparison to LF-HD and HF-HD

The molecular weight of the main component was determined from measurements of osmotic pressure2 and a detailed amino-acid analysis was carried out by the procedure of Moore and Stein3

Myoglobin from equine skeletal muscle Sigma-Aldric

It could be shown that the molecular weights assigned to the SDS-PAGE bands by the companies are incorrect. Arranged in descending order, the marker kits are composed of the following polypeptide fragments from myoglobin: positions 1-153, 1-131, 56-153, 56-131, 1-55, and 132-153. A polypeptide comprising residues 1-14 was not found Metalloprotein Hemoglobin = C2952 H4664 O832 S8 Fe4 (btw numbers are all subscript)- ( letters are the elements). Hope I answered the question Myoglobin is a globular heme protein that serves to store molecular oxygen. It accepts oxygen from the lungs via hemoglobin. In muscles at rest myoglobin is oxygenated. During contraction the demand for oxygen is greatest ; as the intracellular oxygen pressure falls, oxygen dissoci­ ates from myoglobin and is released to cytochrome oxidase low molecular weight proteins to migrate with or in front of the dye front. Protein Molecular Weights (daltons) Protein Molecular Weight Triosephosphate isomerase 26,625 Myoglobin 16,950 α-Lactalbumin 14,437 Aprotinin 6,512 Insulin b chain, oxidized 3,496 Bacitracin 1,423 Reference 1. Schägger, H., and von Jagow, G., Anal. Biochem., 166, 368. /muy euh gloh bin, muy euh gloh /, n. Biochem. hemoglobin of muscle, weighing less and carrying more oxygen and less carbon monoxide than blood hemoglobin. Also, myohemoglobin /muy euh hee meuh gloh bin, hem euh /. [1920 25; MYO + GLOBIN] * *

Unstained Natural Protein Standards | Life Science

Company Telephone: Fax: Hours: Monday to Friday 8:30 - 17:30 PST (GMT-8) Location: 520 Mercury Driv The spatial distribution of the oxygen partial pressure PO 2 (upper panel), myoglobin oxygen saturation (Mb-SO 2, middle panel), and fraction of myoglobin-facilitated oxygen diffusion fO 2fac (lower panel) within the Krogh cylinder is shown. The capillary length is normalized and given in percentages. (A) Distribution during continuous diastolic blood flow; (B) distribution after systolic. molecular properties of myoglobin, the secondary and tertiary structures, as well as the molecular weight size of the protein, were examined after irradiation at various irradiation doses. Gamma-irradiation of myoglobin solutions caused the disruption of the ordered structure of the protein molecules, as well as degradation, cross The molecular weight of Myoglobin was determined to be 18204 Da And 0.423 mg of iron were detected in the acid digested extract Introduction Myoglobin is a globular protein which contains a single polypeptide chain of about 153 amino acids and an iron-porphyrin complex, or the heme group (3)

They were the first to observe the 3d electronic state of Fe in myoglobin, which contains only one Fe atom in its large molecule with a molecular weight of approximately 16500, using the high-brilliance soft X-rays produced at SPring-8. They clarified that the mechanisms behind the storage and release of oxygen by myoglobin depend on the. Download Citation | Myoglobin and Hemoglobin | Hemoglobin is the vital protein that conveys oxygen from the lungs to the tissues and facilitates the return of carbon dioxide from the tissues. The RR of myoglobin was significantly higher with Phylther UP compared to Phylther G (RR of 62% versus 39.8%, p<0.0001). HD with Phylther UP didn't show statistical difference in RR of myoglobin compared to HDF (RR 62% vs 66.1%, p=0.14) (Table2) highly complex substance that is present in all living organisms. Proteins are of great nutritional value and are directly involved in the chemical processes essential for..

Difference Between Haemoglobin and Myoglobin - Difference Wik

volume, the myoglobin in fraction 2 has a molecular weight of 35000 & 1000 (see Fig.2). It therefore seems likely that it is a dimer. A sample of bovine myoglobin, prepared accord- ing to procedure 1, also contained some dimer, though less than horse myoglobin. The elution volumes of the bovine myoglobin monomer and dimer corre

Tech Tips | In search of low molecular weight proteinsNutrients | Free Full-Text | Heme, an Essential Nutrient
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