Amino Acids and Proteins Flashcards
Define the following terms: Isoelectric point
pH at which a molecule carried no net charge.
Define the following terms: Zwitterion
moments of differing charge but net neutral
Define the following terms: Amphoteric
serves as both an acid and base
Define the following terms: Amino acid
essential molecules that build protein
Define the following terms: Peptide bond
from acid group to amino groupof two animo acids
Define the following terms: Complex or conjugated protein
more than 1 combined tertiary structure
Discuss protein structures and classifications
Size: 6k-1m Da
Differential Solubility
Charge (more pos more easily disolved)
Adsorption (ability for water to cling to)
Specific binding to antibodies
Made of C, O, H, N, S. N sets apart from lipids and carbohydrates.
Differentiate among protein structures:
Primary
Chain of amino acids
Differentiate among protein structures:
Secondary
Linked by H-bonds. Beta sheets and Alpha helices. Alpha more common.
Differentiate among protein structures:
Tertiary
Formed when attractions occur between the sheets and helices. Function is related to folding structure
Differentiate among protein structures:
Quaternary
multiple tertiary structures together. Think Hemoglobin.
Explain the process of digestion and absorption of dietary proteins
Pepsin breaking proteins into peptides. Peptides are broken into Amino acids by secretin in the intestines. Pancreas Acinar cells secrete enzymes to assist
State the main physiologic functions of plasma proteins
Albumin: 54%
Globulins: 46%
Total protein - albumin = Globulins
Identify the main site of synthesis for plasma proteins
Prealbumin: Liver and choroid plexus
Albumin: liver
Discuss the degradation of amino acids
Transamination and oxidative deamination
Transamination: the transfer of an amino group from one molecule to another
deamination: the removal of an amino group from an amino acid or other compound
Discuss the degradation of amino acids
Ketogenic and glycogenic amino acids
Ketogenic: can be oxidized to generate acetyl-CoA
glycogenic amino acids: an amino acid that can be converted into glucose
State the electrophoretic fraction in which each is located, the normal function, and disease states associated with abnormal levels
Albumin
Function: oncotic pressure
Disease: Liver disease, renal disease, dehydration, malnutrition
State the electrophoretic fraction in which each is located, the normal function, and disease states associated with abnormal levels
Alpha-1-antitrypsin
Synthesized in: liver
protects elastin in the lungs by inhibiting elastase
diseases: inflammitory disease
State the electrophoretic fraction in which each is located, the normal function, and disease states associated with abnormal levels
Alpha-2-macroglobulin
synthesized in the liver
serine protease inhibitor
Decreased in: acute pancreatitis, prostate cancers, inflam disorders
Increased in: nephrotic syndrome, contraceptive use, pregnancy and estrogen therapy
State the electrophoretic fraction in which each is located, the normal function, and disease states associated with abnormal levels
Haptoglobin
Function: transport protein (free hemoglobin)
increased in: inflam disease, burns, trauma
Decreased in: intravascular hemolysis, liver disorders
State the electrophoretic fraction in which each is located, the normal function, and disease states associated with abnormal levels
Ceruloplasmin
function: transport protein (copper)
increaded in: inflam, severe infection, tissue damage
Decreased in: (primary) Wilson’s disease. (secondary) malnutrition/malabsorption, liver disease, nephrotic syndrome
State the electrophoretic fraction in which each is located, the normal function, and disease states associated with abnormal levels
Transferrin
Function: transport protein (iron)
increased: Iron deficiency
decreased: iron overload
State the electrophoretic fraction in which each is located, the normal function, and disease states associated with abnormal levels
Fibrinogen
Function: clot when activated by thrombin
increased: infection, pregnancy
decreased: coagulation
State the electrophoretic fraction in which each is located, the normal function, and disease states associated with abnormal levels
C-reactive protein
Function: stimulates tissue factor, causing coagulation and activating complement
Should be none
increased: tissue damage
Correlate disease states and disorders associated with total protein levels and other test results
Hypoproteinemia: TP less than ref range. Any condition with a negative Nitrogen balance. Caused by excessive loss, decreased intake/synthesis, or accelerated breakdown of proteins
Hyperproteinemia: TP greater than ref range. Caused by dehydration or overproduction of gamma globulins
State the reference range for serum total protein and albumin.
TP: 6.5-8.3 g/dl in adults
Albumin 3.5-5.5 g/dl
