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    Displaying items by tag: Hemoglobin

    hemoglobin-gentaurThe hemoglobin molecule is composed of four polypeptide chains of the protein globin. In addition, all of these chains contain nonprotein ferruginous material - heme, which has a direct role in the binding and transport of oxygen.

    Globinat is a protein such as albumin, that contain amino acid residues. Hema and globinat influence. Globinat alters the properties of heme so as to bind the oxygen. HEMA provides stability of globin against the action of acids, temperature, the action of enzymes and specific features of the crystallization thereof.

    In adults, 98% of the hemoglobin type A (HbA), in the fetus and newborn is mostly type F (HbF), which in the first days after birth, changes in HbA.

    Congenital disorders and diseases of the hematopoietic system appear abnormal types of hemoglobin as methemoglobin, which is unable to carry oxygen. In blood of healthy persons methaemoglobin in minor amounts. Methaemoglobin binds with hydrocyanic (senile) acid and other substances, so is used in medicine in such poisoning.


    Normal hemoglobin levels in men ranged from 135-160 g / l in women - 120-140 g / l


    Formation and decomposition of hemoglobin
    The biosynthesis of hemoglobin was obtained in young erythrocytes, which penetrate into the iron atoms. Globinat formed from amino acids, i.e. at the usual time of synthesis of proteins.

    Disintegration of hemoglobin begins in erythrocytes, which are at the end of their life cycle. In the process of decomposition to yield derivative verdoglobin having green color. It is unstable and falls apart easily. Heme disintegrates in cells of the liver, bone marrow and spleen to form yellow pigments. In this process, the iron atoms were removed, which again is connected with the erythrocytes to form new molecules heme.


    Properties of hemoglobin
    The main biological role of hemoglobin is its participation in the process of exchange of gaseous substances from the environment and the body. Hemoglobin provides oxygen transport in the blood from the lungs to the tissues and transport of carbon dioxide from the tissues to the lungs. The similarity of the hemoglobin molecule oxide is three times greater than with the oxygen molecules, which determines the properties of high toxic carbon monoxide. Therefore, when the concentration of carbon monoxide in the air of 0,1% more than half of hemoglobin in the blood is not bound with oxygen and carbon monoxide. In this form carboxyhemoglobin which can not transport oxygen.


    Another important function of hemoglobin is that of maintaining the acid-base balance in the body.


    Changes in hemoglobin
    Upon failure of the hemoglobin in erythrocytes disrupting metabolism in cells. Low hemoglobin specific for iron deficiency anemia, which most commonly are caused by chronic blood loss or poor nutrition, especially when excludes the consumption of animal protein.

    High hemoglobin may be normal or physiological phenomenon feature of the disease. For example, in people living in high mountains register compensatory increase in the level of hemoglobin in the blood, due to the reduced content of oxygen in the air.

    Deficiency of some B vitamins leads to changes in the blood with high hemoglobin and decrease the number of red blood cells - malignant anemia. In certain cardiovascular and pulmonary disorders also can be observed high hemoglobin (the number of red blood cells but does not change), since disturbed blood flow in tissues do not receive oxygen.

    Hemoglobin is one of the most important health indicators and indicators of change should seek competent medical opinion.

    Published in News
    Monday, 26 May 2014 10:15

    Erythropoietin, EPO

    Gentaur ErythropoietinI. Definition

    Erythropoietin is glikoproteid hormone that is a growth factor with respect to erythropoiesis . Human erythropoietin is a polypeptide consisting of 165 amino acids. It can stimulate alone or with the participation of other cytokines , growth and development of the precursors of erythrocytes in the bone marrow , causing an increase in the number of red blood cells.

    90% of erythropoietin in adults is synthesized and secreted by interstitial cortical kidney fibroblasts , in response to a reduced supply of oxygen to the tissues . The remaining 10 % of EPO are synthesized by hepatocytes and Ito- interstitial cells of the liver ( relevant in the fetal and perinatal ) . Erythropoietin secretion is controlled by the level of oxygen saturation of the blood. Under conditions of hypoxia ( lack of oxygen to cells and tissues ) , erythropoietin plasma increases. Hypoxia may be caused by anemia , reduced oxygen - carrying capacity , decreased oxygen saturation of the hemoglobin molecules and the like. There is an assumption that there is a reverse correlation between the serum levels of EPO and the amount of red blood cells.
     

    Additional features of EPO nehemopoetichni : can induce vasoconstriction and hypertension associated with that stimulates angiogenesis and proliferation of smooth muscle fibers, may increase the absorption of iron by the inhibition of the hormone hepsidin . Studies have reported that EPO influences neuronal protection in conditions of hypoxia (e.g. stroke , etc.) , improves memory . Administration of EPO may be effective for treating depression.

    II. Test method:

     
    ELISA " sandwich principle." EPO ELISA assay using two different mouse monoclonal antibodies specifically directed against different regions of the human EPO .
     
    III. Content and clinical significance :

    Clinical indications for the study of indicators:
     - Diagnosis and differential diagnosis of anemia and polycythemia ;
     - To help predict and monitor the response to treatment with recombinant erythropoietin in patients with anemia ;

    Quantification of EPO serum aid in the diagnosis and differential diagnosis of anemia and erythrocytosis .


    1. Anemia :
     Aplastic , haemolytic and iron deficiency anemia - the values ​​of EPO were increased ;
     
     Anemia of kidney disease and certain other diseases ( e.g., AIDS), - the values ​​of EPO are low ;

    Low , the concentration of EPO may be an early signal of kidney transplant rejection .

    EPO can also be used for monitoring of patients with AIDS of AZT- therapy . The increase in EPO in these patients is a signal that anemia in ongoing AZT- therapy due to hypoplasia / aplasia of the red blood cell .


    2 . Upon erythrocytosis :
    Polycythemia vera (primary erythrocytosis ) is a result of autonomous proliferation of the 3 lines of blood , with prevalence of erythropoiesis . In these cases, values ​​of EPO are low.


    Secondary polycythemia ( poliglobulii ) if it is off dehydration (relative erythrocytosis ) is due to the increase in EPO ( secondary stimulation eritopoezata ) due to various reasons :
    Individual elevated EPO - in paraneoplastic syndromes ( with hypernephroma , ovarian carcinoma , tumors of the cerebellum and the like . , In these cases, the EPO may be used as a tumor marker ) in polycystic kidney disease , familial erythrocytosis ;
     
    Compensatory increase in EPO - in hypoxia (residing at high altitudes , pulmonary disease , heart disease ) , Disability hemoglobin ( congenital methemoglobinemia , carboxyhemoglobin ) medications ;

    For diagnostic purposes , the test results should always be assessed in accordance with the patient's history , clinical and other studies .
     
    IV. Material for testing : serum

    Important requirements for sampling : it is blood clotting retrahirane clot to become 2 - 8 ° C or on ice. Samples coagulated at room temperature can produce lower amounts of EPO . The separated serum after centrifugation was frozen at -15 ° C or lower temperature , and thus is transported , if needed.

    Published in News

    Tibetan-dog-brucella-anti-elisa-anti-human

    See Spot run. See Lassie save Timmy from a well. See Tibetan Mastiffs climb 4,500 meters above sea level on the Tibetan Plateau. The ever-so-fluffy Tibetan Mastiff, which commonly serves as a guard dog for the plateau's residents, is able to breathe comfortably at high altitudes. Like the Tibetan people, Tibetan Mastiffs have adapted to air with less oxygen.

    Ya-Ping Zhang and a team of scientists examined sets of genes from 32 Tibetan Mastiffs, 20 Chinese native dogs, and 14 wolves to investigate how the Mastiffs have adjusted. They looked for variations in the DNA sequence called single-nucleotide polymorphisms (SNPs, also pronounced simply as "snips"). The scientists genotyped the SNPs in the Mastiffs and compared them to the ones in the dogs and wolves.

    After finding more than 120,000 SNPs, Zhang and the scientists identified 16 genes with signals of positive selection in the Tibetan Mastiff – 12 of these genes are connected to functions in the body that would help the canine adapt to high altitudes with low oxygen levels. Several of these genes are responsible for the building of hemoglobin, which helps transport oxygen through blood, and monitoring metabolism. Oxygen is required to process consumed food into energy, so efficient metabolizing means less oxygen is used. One of the genes, EPAS1, has also been linked to helping Tibetan humans adapt to high altitudes.

    Published in News

    2D and Criterion-anti-suman-elisa

    - Hemoglobin voids in flow-through >98%, with <30 minute bind/wash/elute protocol

    - Hemoglobin removal from red cell lysates for RBC proteomics

    - Hemoglobin removal from hemolyzed serum, blood and dried blood spot/blood card

    - Enrichment of hemoglobin variants.

    - Low abundance protein and enzyme enrichment

    - Disposable, cost-effective and high-throughput

    - Mild elution maintains tertiary structure and simple transfer to secondary analysis

    - Removes hemoglobin from species including human, sheep, bovine, goat, etc.

    - Removes hemoglobin from organs, tissues.

    - The eluted fractions retain their enzymatic and biological activity

    - The eluted fraction is compatible with LC-MS, activity based protein profiling and proteomic studies.

    HemoVoid™ , a silica-based protein enrichment matrix, removes hemoglobin from erythrocyte lysate samples while concentrating low abundance, and/or low molecular weight proteins. The HemoVoid™ protocol uses mild buffers; the protocol conditions are so gentle that native enzyme activity is retained in elution fractions.

    HemoVoid™ derives from a silica-based library of individual mixed-mode ligand combinations (ionic, hydrophobic, aromatic, polymer). The library was designed to facilitate weak binding of proteins, allowing for rapid elution from the matrix without any foreknowledge of the variety of proteins contained in the starting sample. HemoVoid™ depletes hemoglobin from red cell lysates while improving the resolution of less abundant blood proteins.

     PDF-IconDownload datasheet: HemoVoid™ - Hemoglobin Depletion From Erythrocytes

    Product list:

    Cat. Product Quantity Promo Price Order
    HVK-05 HemoVoid™, Hemoglobin Depletion 5 mL 291 € Order
    HVK-10 HemoVoid™, Hemoglobin Depletion 10 mL 382 € Order
    HVK-50 HemoVoid™, Hemoglobin Depletion 50 mL 1300 € Order
    HVK-100 HemoVoid™, Hemoglobin Depletion 100 mL 2029 € Order
    Published in Promos

    HemogloBind2

    - Has a high degree of specificity for hemoglobin binding up to 10 mg/ml

    - Applications in blood substitutes, enzyme recovery and analytical interferences

    - Removes hemoglobin from any species including human, sheep, bovine, goat, etc

    - Removes hemoglobin from organs, tissues.

    - Hemoglobin removal from red blood cell lysate for proteomics and biomarker drug discovery

    - The flow through fractions retain their enzymatic and biological activity

    - The flow through fractions is compatible with LC-MS, activity based protein profiling and proteomic studies.

    HemogloBind™ comes from a class of solid-phase, or surface-based, elastomeric poly-electrolytic surfaces that bind proteins through an empirically derived chemistry combining elements of polymer composition, cross-linking architecture and charge properties. HemogloBind™ is engineered for a high degree of selectivity and does not cross react with most common serum components, making it an excellent tool in numerous applications. These include analytical protocols where optical interference is problematic, such as bilirubin analysis and bulk serum clarification. Hemoglobin variants, as in thalassemia, bind with differential affinity towards HemogloBind™. For purification and/or analysis of hemoglobin, a modest elevation in pH will facilitate desorption of hemoglobin bound to HemogloBind

    PDF-IconDownload datasheet: HemogloBind™ Hemoglobin Depletion From Hemolyzed Serum/Plasma

    Product list:

    Cat. Product Quantity Promo Price Order
    H0145-05 HemogloBind™ , Hemoglobin Depletion From Hemolyzed Serum/Plasma 5 mL 278 € Order
    H0145-15 HemogloBind™ , Hemoglobin Depletion From Hemolyzed Serum/Plasma 15 mL 400 € Order
    H0145-50 HemogloBind™ , Hemoglobin Depletion From Hemolyzed Serum/Plasma 50 mL 773 € Order
    H0145-15-60P HemogloBind™ , Hemoglobin Depletion From Hemolyzed Serum/Plasma 15 mL (60 Aliquots of 250 ul HemogloBind each) 616 € Order
    H0145-50-200P HemogloBind™ , Hemoglobin Depletion From Hemolyzed Serum/Plasma 50 mL (200 Aliquots of 250 ul HemogloBind each) 1188 € Order
    Published in Promos

    131208133646-elisa-kits-assay-kitsHematology researchers at The Children's Hospital of Philadelphia have manipulated key biological events in adult blood cells to produce a form of hemoglobin normally absent after the newborn period. Because this fetal hemoglobin is unaffected by the genetic defect in sickle cell disease (SCD), the cell culture findings may open the door to a new therapy for the debilitating blood disorder.
    "Our study shows the power of a technique called forced chromatin looping in reprogramming gene expression in blood-forming cells," said hematology researcher Jeremy W. Rupon, M.D., Ph.D., of The Children's Hospital of Philadelphia. "If we can translate this approach to humans, we may enable new treatment options for patients."
    Rupon presented the team's findings today at a press conference during the annual meeting of the American Society of Hematology (ASH) in New Orleans. Rupon worked in collaboration with a former postdoctoral fellow, Wulan Deng, Ph.D., in the laboratory of Gerd Blobel, M.D., Ph.D.
    Hematologists have long sought to reactivate fetal hemoglobin as a treatment for children and adults with SCD, the painful, sometimes life-threatening genetic disorder that deforms red blood cells and disrupts normal circulation.
    In the normal course of development, a biological switch flips during the production of hemoglobin, the oxygen-carrying component of red blood cells. Regulatory elements in DNA shift the body from producing the fetal form of hemoglobin to producing the adult form instead. This transition occurs shortly after birth. When patients with SCD undergo this transition, their inherited gene mutation distorts adult hemoglobin, forcing red blood cells to assume a sickled shape.
    In the current study, Rupon and Blobel reprogrammed gene expression to reverse the biological switch, causing cells to resume producing fetal hemoglobin, which is not affected by the SCD mutation, and produces normally shaped red blood cells.
    The scientists built on previous work by Blobel's team showing that chromatin looping, a tightly regulated interaction between widely separated DNA sequences, drives gene transcription -- the conversion of DNA code into RNA messages to carry out biological processes.
    In the current study, the researchers used a specialized tool, a genetically engineered zinc finger (ZF) protein, which they custom-designed to latch onto a specific DNA site carrying the code for fetal hemoglobin. They attached the ZF to another protein that forced a chromatin loop to form. The loop then activated gene expression that produced embryonic hemoglobin in blood-forming cells from adult mice. The team obtained similar results in human adult red blood cells, forcing the cells to produce fetal hemoglobin.
    Rupon and Blobel will continue investigations aimed at moving their research toward clinical application. Rupon added that the approach may also prove useful in treating other diseases of hemoglobin, such as thalassemia.

    Published in News