TORCH complex

(noun)

TORCH complex is a medical acronym for a set of perinatal infections (which are infections that are passed from a pregnant woman to her fetus).

Related Terms

  • haematogenous
  • petechial

Examples of TORCH complex in the following topics:

  • The TORCH Panel of Tests

    • TORCH complex is a medical acronym for a set of perinatal infections (which are infections passed from a pregnant woman to her fetus).
    • TORCH infections can lead to severe fetal anomalies or even fetal loss.
    • The TORCH panel of tests acronym spells out as follows:
    • Symptoms of a TORCH infection may include fever and difficultly feeding.
    • Hearing impairment, eye problems, mental retardation, autism, and death can be caused by TORCH infections.
  • Immune Complex Autoimmune Reactions

    • An immune complex is formed from the integral binding of an antibody to a soluble antigen and can function as an epitope.
    • An immune complex is formed from the integral binding of an antibody to a soluble antigen.
    • Immune complexes may cause disease when they are deposited in organs, e.g. in certain forms of vasculitis.
    • Type III hypersensitivity reactions are immune complex-mediated.
    • An immune complex is formed from the integral binding of an antibody to a soluble antigen.
  • Siderophores

    • The ability to form water soluble Fe3+ complexes is a key component to the active transport of the Fe-siderophore complex across the cellular membrane.
    • The complexes then generally bind to the cellular membrane using cell specific receptors.
    • In areas of low iron, the organism will release yersiniabactin to form Fe3+ complexes.
    • Once the enterobactin-Fe3+ complex arrives intracellularly, it is necessary to remove the Fe3+ from the complex.
    • The iron released from the complex will then be utilized in metabolic processes.
  • Complex and Asymmetrical Virus Particles

    • Complex viruses are often asymetrical or symetrical in combination with other structures such as a tail.
    • The poxviruses are large, complex viruses that have an unusual morphology.
    • Some viruses that infect archaea have complex structures unrelated to any other form of virus.
    • T4 is a bacteriophage that infects E. coli and is referred to as a complex virus.
    • Although it has an icosahedral head, its tail makes it asymmetrical, or complex in terms of structure.
  • Type III (Immune Complex) Reactions

    • When these antigens bind antibodies, immune complexes of different sizes form.
    • Large complexes can be cleared by macrophages but macrophages have difficulty in the disposal of small immune complexes.
    • These immune complexes insert themselves into small blood vessels, joints, and glomeruli, causing symptoms.
    • Often, immunofluorescence microscopy can be used to visualize the immune complexes.
    • An immune complex is formed from the integral binding of an antibody to a soluble antigen.
  • T Cell Receptors

    • MHC molecules and peptides form complexes on the surface of antigen presenting cells (APCs).
    • The receptor that recognizes these peptide-MHC complexes is called the T Cell Receptor (TCR).
    • The biochemical signals that are triggered in T cells following antigen recognition are transduced not by the TCR itself, but by invariant proteins (CD3, and zeta), which are non-covalently linked to the antigen receptor to form the TCR complex.
    • The physiologic role of some accessory molecules is to deliver signals to the T cells that function in concert with signals from the TCR complex to fully activate the cell.
    • The recognition of peptide-MHC complexes is mediated by CDRs formed by both the alpha and beta chains of the TCR.
  • Substrates for Biosynthesis

    • Major metabolic pathways require substrates to be acted upon for the formation of larger, more complex products.
    • The major metabolic pathways require substrates to be acted upon for the formation of larger, more complex products.
    • Biosynthetic processes are defined by the production of more complex products that are required for growth and maintenance of life.
    • These precursors are used as substrates for the biogenesis of large complex products.
  • DNA Mobility Shifts

    • An antibody that recognizes the protein can be added to this mixture to create an even larger complex with a greater shift.
    • This method is referred to as a supershift assay, and is used to unambiguously identify a protein present in the protein-nucleic acid complex.
    • Lane 3 contains protein and a DNA fragment that does react; the resulting complex is larger, heavier, and slower-moving.
    • The pattern shown in lane 3 is the one that would result if all the DNA were bound and no dissociation of complex occurred during electrophoresis.
    • When these conditions are not met a second band might be seen in lane 3 reflecting the presence of free DNA or the dissociation of the DNA-protein complex.
  • Biosynthesis of Tetrapyrroles

    • Porphyrins are the conjugate acids of ligands that bind metals to form complexes.
    • Complexes of meso-tetraphenylporphyrin, e.g., the iron(III) chloride complex (TPPFeCl), catalyze a variety of reactions in organic synthesis.
    • For example, complexes of meso-tetraphenylporphyrin, e.g., the iron(III) chloride complex (TPPFeCl), catalyze a variety of reactions of potential interest in organic synthesis.
    • Porphyrins are the conjugate acids of ligands that bind metals to form complexes.
  • Mapping Protein-Protein Interactions

    • In living organisms most of the biological functions are mediated by complex multi-component protein machineries and network activities.
    • The protein complexes formed could be stable (proteins interact for a prolonged period of time) or transient (proteins interact for a brief period of time).
    • Molecular studies are necessary to dissect the constituents of these protein complexes and identify the domains through which a protein interacts with another.
    • Purified protein complexes are then resolved on native gels and discrete protein bands are excised and digested into small peptide fragments by trypsin.
    • Results collected from binary and co-complex experiments are documented into a database.
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