Proteins and Tumor Markers

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Author:
ncrook
ID:
204453
Filename:
Proteins and Tumor Markers
Updated:
2013-05-03 01:35:06
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Plasma Total Protein Classification
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Plasma Total Protein, Classification
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  1. What organ synthesizes most of the plasma proteins?
    Liver
  2. What cells synthesize the immunoglobulins?
    Plasma cells
  3. What do the plasma cells synthesize?
    Immunoglobulins
  4. What happens when proteins degrade?
    Their consituent amino acids undergo deamination with the formation of ammonia - which is converted to urea for excretion in the urine
  5. What is released at the site of injury or inflammation and what does it cause?
    Some cytokines are released, causing the liver to increase synthesis of the acute-phase reactant proteins
  6. What are negative acute-phase proteins?
    Some proteins that decrease in concentration when an injury or inflammation is occurring
  7. What are immunoglobulins?
    Humoral antibodies produced in response to foreign antigens for the purpose of destroying them
  8. What is the reference range for Total Protein?
    6.5-8.3 g/dL
  9. What is the reference range for albumin?
    3.5-5.0 g/dL
  10. What causes Hypoproteinemia?
    • Urinary loss
    • Gastrointestinal tract inflammation
    • Liver disorders
    • Malnutrition
    • Inherited immunodeficiency disorders
    • Extensive burns
  11. What causes Hyperproteinemia?
    • Dehydration
    • Increased protein production (assoc w/monoclonal and polyclonal gammopathies)
    • Chronic inflammatory diseases associated with paraprotein production
  12. What is the term for polypeptides composed of only amino acids?
    Simple proteins
  13. What is the term for symmetrical, compactly folded polypeptide chains (e.g. albumin)?
    Globular proteins
  14. What is the term for elongated, asymmetrical polypeptide chains (e.g. troponin and collagen)?
    Fibrous proteins
  15. What is the term for the protein that is composed of protein (apoprotein) and nonprotein (prosthetic group) components?
    Conjugated proteins
  16. What are prosthetic groups commonly, in nature?
    • Metal
    • Lipid
    • Carbs
  17. What is the term ofr a protein with a metal prosthetic group (e.g. ceruloplasmin)?
    Metalloprotein
  18. What is the term for a protein with a lipid prosthetic group (e.g. cholesterol, triglyceride)?
    Lipoprotein
  19. What is the term for a protein with 10-40% carbohydrates attached (e.g. haptoglobin)?
    Glycoprotein
  20. What is the term for a protein with >40% carbohydrates attached (e.g. mucin)?
    Mucoprotein
  21. What is the term for a protein with DNA or RNA nucleic acids attached (e.g. chromatin)?
    Nucleoprotein
  22. What is the term for when proteins can be broken down into amino acids that can be used in the citric acid cycle to produce energy?
    Energy production
  23. What is the term for maintaining the colloidal pressure between differend body compartments?
    Water distribution
  24. What is the term for the ionizable R groups of the individual amino acids of a protein that provide buffering capacity by binding or releasing H+ ions as needed?
    Buffer
  25. What is the term for binding of proteins to hormones, free hemoglobin, lipids, drugs, calcium, unconjugated bilirubin, and so on, allows movement of these and other molecules in the circulation?
    Transporter
  26. What is the term for proteins that protect the body against "foreign" invaders?
    Antibodies
  27. What is the term for the proteins that function as receptors for hormones so that the hormonal message can activate cellular components?
    Cellular proteins
  28. Name some examples of cellular proteins that are considered hormones, but proteins in nature
    • ACTH
    • FSH
    • LH
    • TSH
  29. What is the term for collagen is the fibrous component that maintains the structure of body parts such as skin, bone, cartilage, and blood vessels?
    Structural proteins
  30. What is the term for catalysts that accelerate chemical reactions?
    Enzymes
  31. Proteins are made of what and how are they linked together?
    • Made of amino acids
    • Each amino acid being linked to another via a peptide bond
  32. How is a peptide bond formed?
    When the Carboxyl (-COOH) group of one amino acid links to the amino (-NH2) group of another amino acid with the loss of a water molecule
  33. What is the term for the end of the protein structure with a free amino group?
    N-terminal
  34. What is the term for the end of a protein structure with a free carboxyl group?
    C-terminal
  35. What makes proteins different from carbs and lipids?
    Proteins consist of 16% nitrogen
  36. What is structure occurs when the amino acids are linked to each other through covalent peptide bonding in a specific sequence to form a polypeptide chain?
    Primary structure
  37. What structure occurs when the polypeptide chain winds to form alpha helixes and beta sheets through the formation of hydrogen bonds between CO and NH groups of the peptide bonds?
    Secondary structure
  38. What structure occurs when the coiled polypeptide chain folds upon itself to form a 3-D structure through the interactions of the R groups of the amino acids?
    Tertiary structure
  39. What structure occurs when 2 or more folded polypeptide chains bind to each other through hydrogen bonds and electrostatic interactions to form a functional protein?
    Quaternary structure

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