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AAs, Proteins, NNCs
Amino Acids, Proteins, and Non Nitrogen Compounds
| Question | Answer |
|---|---|
| What are amino acids? | Building blocks of protein essential for cellular growth, repair, and maintenance |
| What is the basic structure of a single amino acid? | Contains one amino group and one carboxyl functional group. |
| What is a peptide bond? | The bond formed between the amino group of one amino acid and the carboxyl group of another. |
| What is a polypeptide? | A chain of amino acids linked by peptide bonds. |
| What defines a protein? | A large polypeptide that is composed of one or more polypeptide chains. |
| List three essential amino acids. | Isoleucine, Leucine, Lysine. |
| What is the role of branched-chain amino acids? | Essential for muscle tissue, wound healing, and glucose homeostasis. |
| What is the function of Arginine (Arg)? | Important for cell division, wound healing, protein synthesis, and hormone release. |
| What is the significance of Histidine (His)? | Needed for tissue repair, myelin sheath maintenance, and as a precursor of histamine. |
| What role does Lysine (Lys) play in the body? | Involved in antibody production, calcium absorption, and collagen formation. |
| What is Methionine (Met) known for? | Initiates translation of mRNA and acts as an important cellular antioxidant. |
| What is Phenylalanine (Phe) a precursor for? | Catecholamines such as norepinephrine, epinephrine, and dopamine |
| What is Threonine (Thr) important for? | Formation of collagen, elastin, and maintaining protein balance in the body. |
| What is Tryptophan known for? | Metabolic precursor to serotonin and melatonin, helps alleviate insomnia and anxiety. |
| List three non-essential amino acids. | Alanine, Asparagine, Aspartic acid. |
| What is the role of Alanine? | Product of DNA breakdown and involved in the metabolism of amino acids. |
| What is the function of Glycine? | Involved in the synthesis of proteins and neurotransmitters. |
| What is the importance of Glutamine? | Supports immune function and intestinal health. |
| What is the role of Serine? | Involved in the synthesis of proteins and metabolism of fats. |
| What is the significance of Tyrosine? | Precursor for neurotransmitters and hormones, important for mental health. |
| What is the primary role of amino acids formed from glucose metabolism in muscle tissue? | They play a major role in the transfer of nitrogen from peripheral tissues to the liver for processing and excretion. |
| What are non-essential amino acids? | Amino acids that can be synthesized by the body and are not required in the diet. |
| What is asparagine derived from? | Aspartic acid and ATP through transamination. |
| What is the primary function of asparagine? | Conversion of one amino acid into another via amination or transamination. |
| What is the significance of aspartic acid in metabolism? | It is a precursor for several other amino acids and participates in gluconeogenesis. |
| What is the role of cysteine in the body? | It is an important structural and functional component of many proteins and enzymes. |
| What neurotransmitter is associated with glutamic acid? | It serves as a neurotransmitter and dysregulation has been linked to epileptic seizures. |
| What is glutamine's role in the body? | It aids in renal maintenance of acid-base balance and provides fuel for the digestive tract. |
| What is glycine essential for? | Synthesis of nucleic acids, bile acids, proteins, and other important biomolecules. |
| What is the function of proline in the body? | It is involved in wound healing and works with vitamin C to promote healthy connective tissues. |
| What role does serine play in metabolism? | It is needed for the metabolism of lipids and fatty acids and aids in the production of antibodies. |
| What is tyrosine synthesized from? | |
| It is metabolically synthesized from phenylalanine. | |
| What is phenylketonuria (PKU)? | |
| An autosomal recessive disorder caused by the absence of phenylalanine hydroxylase, leading | |
| to high levels of phenylalanine. | |
| What is the Guthrie test used for? | |
| It is a screening test for phenylketonuria based on the ability of phenylalanine to facilitate | |
| bacterial growth. | |
| What is Type I Tyrosinemia? | |
| The most severe form of tyrosinemia, affecting the liver and kidneys, caused by a mutation in | |
| the FAH gene. | |
| What are the symptoms of alkaptonuria? | |
| Dark blue-black pigmentation in cartilage and degenerative arthritis due to elevated ho | |
| mogentistic acid. | |
| What is the metabolic defect in Maple Syrup Urine Disease? | |
| A mutation that inhibits the metabolism of leucine, isoleucine, and valine due to reduced | |
| activity of branched-chain alpha-ketoacid dehydrogenase. | |
| What is Isovaleric Acidemia characterized by? | |
| A distinctive odor of 'sweaty feet' due to the buildup of isovaleric acid. | |
| What is the most common form of Homocystinuria caused by? | |
| Mutations in the CBS gene leading to cystathionine beta synthase deficiency. | |
| What is Citrullinemia? | |
| A urea cycle disorder caused by a mutation in the ASSI gene, leading to elevated citrulline and | |
| ammonia levels. | |
| What are the major functions of proteins? | |
| Catalyzing biochemical reactions, transporting metals, acting as hormone receptors, providing | |
| structure, and participating in immune responses. | |
| What are the four distinct levels of protein structure? | |
| Primary, secondary, tertiary, and quaternary structures. | |
| What is the isoelectric point (pI) of a protein? | |
| The pH at which the protein has no net charge. | |
| What causes denaturation of proteins? | |
| Heat, strong acids or alkalis, enzymatic reactions, exposure to urea, or UV light. | |
| What determines a protein's solubility? | |
| The charge on its surface; proteins are least soluble at their isoelectric point. | |
| What are the ionizable groups in proteins? | |
| Acidic groups (like glutamate) and basic groups (like lysine) that can affect the protein's | |
| charge. | |
| What is the typical composition of a protein? | |
| Proteins consist of carbon, oxygen, hydrogen, nitrogen, and sulfur. | |
| What is the role of enzymes in proteins? | |
| Enzymes catalyze biochemical reactions. | |
| What is the significance of the tertiary structure of a protein? | |
| It determines the protein's three-dimensional shape and its functional properties. | |
| What is the primary structure of a protein? | |
| The specific sequence of amino acids determined by DNA coding. | |
| Where are most plasma proteins synthesized? | |
| In the liver by hepatocytes. | |
| What determines the amino acid sequence in proteins? | |
| The corresponding sequence of bases in the DNA contained in a specific gene. | |
| What is a codon? | |
| A set of three nucleotides that form the genetic code. | |
| How many possible codons are there? | |
| 64 possible codons. | |
| What is transcription in protein synthesis? | |
| The process where double-stranded DNA unfolds in the nucleus to form a complementary | |
| strand of mRNA. | |
| What occurs during translation? | |
| mRNA is used as a template for protein synthesis by ribosomes in the cytoplasm. | |
| What is the role of tRNA in protein synthesis? | |
| tRNA carries specific amino acids to the ribosome and matches them to the corresponding | |
| codon on mRNA. | |
| What is positive nitrogen balance? | |
| When nitrogen intake exceeds nitrogen loss, often seen in pregnant women and growing | |
| children. | |
| What is negative nitrogen balance? | |
| Occurs when nitrogen loss exceeds intake, often due to tissue destruction or starvation. | |
| What are enzymes? | |
| Proteins that catalyze biochemical reactions. | |
| What are hormones in the context of proteins? | |
| Chemical messenger proteins that control the action of specific cells or organs. | |
| What is the primary function of transport proteins? | |
| To transport ions across biological membranes. | |
| What are immunoglobulins? | |
| Proteins produced by B cells that mediate the humoral immune response. | |
| What do structural proteins do? | |
| Provide structure to cells and tissues, examples include collagen and keratin. | |
| What is the function of storage proteins? | |
| To serve as reservoirs for metal ions and amino acids. | |
| How do proteins contribute to osmotic force? | |
| Their size prevents them from crossing capillary membranes, affecting fluid balance. | |
| What are simple proteins? | |
| Proteins containing only peptide chains of amino acids, can be globular or fibrous. | |
| What are compound (conjugated) proteins? | |
| Proteins that consist of an apoprotein and a non-protein prosthetic group. | |
| What is albumin? | |
| The most abundant plasma protein, responsible for 80% of colloid osmotic pressure. | |
| What is the main function of prealbumin? | |
| Transport of thyroid hormones and an indicator of protein nutrition. | |
| What is alpha 1-antitrypsin? | |
| A serine protease inhibitor synthesized in the liver, important for inhibiting protease activity. | |
| What does an increase in alpha 1-antitrypsin indicate? | |
| Inflammatory reactions, pregnancy, and contraceptive use. | |
| What is alpha-fetoprotein (AFP)? | |
| A protein synthesized in utero, used as a marker for fetal development and certain conditions. | |
| What does an elevated level of AFP indicate? | |
| Conditions like spina bifida and neural tube defects. | |
| What is haptoglobin? | |
| A protein that binds free hemoglobin to prevent iron loss in hemolytic anemia. | |
| What role does ceruloplasmin play? | |
| It is involved in plasma reduction and oxidation reactions and contains copper. | |
| What is the function of inter-alpha-trypsin inhibitors? | |
| They play a role in inflammation and carcinogenesis. | |
| What is the significance of Gc-globulin? | |
| It is a major carrier protein for vitamin D and indicates survival in tissue injury. | |
| What is a positive acute phase reactant? | |
| A substance that is elevated in response to inflammation, severe infection, and tissue damage. | |
| What is the role of serum albumin? | |
| To maintain colloidal osmotic pressure in the peripheral blood. | |
| What condition is characterized by Kayser-Fleischer rings? | |
| Wilson's disease. | |
| What is the function of alpha-2 macroglobulin? | |
| Inhibits proteases such as trypsin and thrombin, useful in evaluating renal disease. | |
| What is transferrin also known as? | |
| Siderophilin. | |
| What does hemopexin bind? | |
| Free heme. | |
| What is the primary function of lipoproteins? | |
| To transport cholesterol, triglycerides, and phospholipids in the bloodstream. | |
| What is beta-2 microglobulin (B2M) associated with? | |
| Impaired clearance by the kidney or overproduction in inflammatory diseases. | |
| What is the most abundant complement protein? | |
| Complement C3. | |
| What does an elevation in C3 and C4 indicate? | |
| Acute inflammatory disease and tissue inflammation. | |
| What is fibrinogen's role in the blood? | |
| To form fibrin clots when activated by thrombin. | |
| What is C-Reactive Protein (CRP) an indicator of? | |
| Inflammatory disease, such as infection or trauma. | |
| What does High Sensitivity CRP (hsCRP) measure? | |
| Risk of cardiovascular disease at levels below 1mg/L. | |
| What are immunoglobulins (Igs) primarily produced by? | |
| B cells that confer humoral immunity. | |
| What are the five classes of immunoglobulins? | |
| IgG, IgM, IgE, IgA, IgD. | |
| What is the function of the constant region in antibodies? | |
| Involved in complement binding and placental passage. | |
| What is class switching in immunoglobulins? | |
| The biological mechanism that changes an antibody from one class to another. | |
| What is the Fab region of an immunoglobulin? | |
| The tip of the 'Y' shape that binds to the antigen. | |
| What is the Fc region of an immunoglobulin responsible for? | |
| Mediating different physiological effects including opsonization and cell lysis. | |
| What is maple syrup urine disease characterized by? | |
| An increase in valine, leucine, and isoleucine. | |
| What does serum haptoglobin bind? | |
| Free hemoglobin. | |
| What is IgG's role in the immune response? | |
| Acts on bacteria and fungi by agglutination and neutralizing toxins. | |
| What is the main function of IgA? | |
| Found in mucous secretions, protecting mucosa from bacteria and viruses. | |
| What is the first antibody to appear in response to an antigen? | |
| IgM. | |
| What is the specific function of IgD? | |
| Unknown, but thought to help regulate B-cell function. | |
| What is the role of IgE in the immune system? | |
| Associated with allergic and anaphylactic reactions. | |
| What is myoglobin used for in clinical settings? | |
| To rule out acute myocardial infarction (AMI). | |
| What are cardiac troponins (cTn) specific to? | |
| Cardiac muscle, used as a gold standard for diagnosing acute coronary syndrome. | |
| What is the typical time frame for protein elevation after onset? | |
| Elevates within 3 to 12 hours of onset, peaks within 12 to 24 hours, and remains elevated for | |
| 3 weeks. | |
| What assay methods are used to measure proteins? | |
| Measured using ELISA or immunoenzymometric assays with 2 monoclonal antibodies directed | |
| against different epitopes. | |
| What are the major components of the natriuretic peptide family? | |
| Atrial natriuretic peptide (ANP), Brain natriuretic peptide (BNP), C-type natriuretic peptide | |
| (CNP), and Dendroaspis natriuretic peptide (DNP). | |
| Where are NT-proBNP and BNP found in greatest concentration? | |
| In the left ventricular myocardium. | |
| What is fetal fibronectin (fFN) used for? | |
| To help predict the short-term risk of premature delivery. | |
| When is fetal fibronectin normally detectable? | |
| In amniotic fluid and placental tissue during early pregnancy; not detectable after 24 weeks. | |
| What is Cystatin C a marker for? | |
| Glomerular filtration rate and is used as an alternative to creatinine. | |
| What is amyloid? | |
| Insoluble fibrous protein aggregates formed due to alterations in their secondary structure, | |
| causing organ failure. | |
| What is hypoproteinemia? | |
| Total protein concentration below the reference interval, occurring due to excessive loss, | |
| decreased synthesis, or increased catabolism. | |
| What are common causes of hypoproteinemia? | |
| Renal disease, GI tract inflammation, blood loss, malnutrition, maldigestion, and accelerated | |
| catabolism due to burns or trauma. | |
| What is hyperproteinemia? | |
| Increase in total protein plasma not associated with disease state, often caused by dehydration | |
| or excessive production. | |
| What is the most common method for total nitrogen analysis? | |
| Chemiluminescence. | |
| What specimen is preferred for determining total protein concentration? | |
| Serum is the specimen of choice. | |
| What method is most widely used for total protein determination? | |
| Biuret method. | |
| How is the A/G ratio calculated? | |
| A/G ratio = albumin / globulins. | |
| What does a decreased A/G ratio indicate? | |
| It may result from decreased albumin or increased globulin. | |
| What is the principle behind electrophoresis? | |
| It separates proteins based on their electric charge and density. | |
| What is Serum Protein Electrophoresis (SPE) used for? | |
| To separate major serum proteins and identify abnormalities. | |
| What does capillary electrophoresis involve? | |
| Separation of molecules in silica capillaries. | |
| What is the clinical application of isoelectric focusing? | |
| To separate proteins based on their isoelectric point. | |
| What indicates the presence of urinary protein? | |
| Proteins appear in urine when they pass through the renal glomerulus and are not reab | |
| sorbed. | |
| What conditions are associated with increased CSF total protein? | |
| Bacterial, viral, fungal meningitis, traumatic lumbar puncture, multiple sclerosis, and neo | |
| plasms. | |
| What is the significance of low CSF protein? | |
| Found in conditions like hyperthyroidism and CNS leakage. | |
| What is the turbidity method used for? | |
| Qualitative testing for proteinuria. | |
| What is the common method for quantitative testing of urinary protein? | |
| Timed urine collection over 12-24 hours. | |
| What are Nonprotein Nitrogen (NPN) Compounds? | |
| Compounds traditionally used to monitor renal function, originating from the need to analyze | |
| nitrogen-containing compounds after protein removal. | |
| How are NPN compounds quantified? | |
| By converting nitrogen to ammonia and reacting it with Nessler's reagent to produce a yellow | |
| color. | |
| What is the primary NPN compound found in blood? | |
| Urea | |
| How is urea formed? | |
| From amino groups (-NH2) and free ammonia generated through protein metabolism in the | |
| liver. | |
| What is the main function of urea in the body? | |
| To serve as a major excretory product of protein metabolism. | |
| Where is urea synthesized and where is it filtered? | |
| Synthesized in the liver and filtered by the kidneys. | |
| What is the normal reference interval for urea nitrogen in adults in plasma or serum? | |
| 6 to 20 mg/dL (2.1 to 7.1 mmol/L) | |
| What is azotemia? | |
| Elevated concentration of urea in blood. | |
| What is uremia? | |
| Very high plasma urea concentration associated with renal failure, also known as uremic | |
| syndrome. | |
| What are the three main categories of azotemia? | |
| Prerenal, renal, and postrenal azotemia. | |
| What causes prerenal azotemia? | |
| Reduced renal blood flow due to factors like CHF, shock, or dehydration. | |
| What is uric acid a product of? | |
| The catabolism of purine nucleic acids. | |
| What happens to most uric acid in the body? | |
| It is reabsorbed in proximal tubules and reused. | |
| What are the clinical applications of measuring uric acid? | |
| Assessment of inherited disorders of purine metabolism, diagnosis and monitoring of gout, | |
| and detection of kidney dysfunction. | |
| What analytical methods are used for measuring uric acid? | |
| Caraway method, uricase methods, coupled enzyme methods, and isotope dilution mass | |
| spectrometry. | |
| What specimen types can be used to measure uric acid? | |
| Heparinized plasma, serum, or urine. | |
| What factors can interfere with uric acid measurement? | |
| High bilirubin concentration, significant hemolysis, and gross lipemia. | |
| What is the role of urea in evaluating renal function? | |
| It helps assess hydration status, nitrogen balance, adequacy of dialysis, and aids in diagnosing | |
| renal disease. | |
| What happens to urea in the kidneys? | |
| Most urea in glomerular filtrate is excreted in urine, but some is reabsorbed in renal tubules. | |
| What is the consequence of high uric acid concentrations? | |
| It can lead to deposition in joints and tissues, causing painful inflammation. | |
| What is the significance of measuring urea in urine? | |
| To evaluate nitrogen excretion and renal function over a 24-hour period. | |
| What is the normal reference interval for urea in a 24-hour urine sample? | |
| 12 to 20 g/d (0.43 to 0.71 mol urea/d) | |
| What drugs have been shown to increase uric acid levels? | |
| Salicylates and thiazides | |
| What is the normal reference interval for uric acid in adult males (plasma/serum)? | |
| 3.5 to 7.2 mg/dL | |
| What is the normal reference interval for uric acid in adult females (plasma/serum)? | |
| 2.6 to 6.0 mg/dL | |
| What is the normal 24-hour urine uric acid excretion for adults? | |
| 250 to 750 mg/day | |
| What condition is characterized by elevated levels of uric acid? | |
| Hyperuricemia | |
| Name one inherited disorder of purine metabolism. | |
| Lesch-Nyhan syndrome | |
| What is gout? | |
| A disease characterized by pain and inflammation of the joints due to precipitation of sodium | |
| urates. | |
| At what age is gout typically diagnosed? | |
| Between ages 30 and 50 years | |
| What is creatinine formed from? | |
| Creatine and creatine phosphate in muscle | |
| What does plasma creatinine concentration indicate? | |
| It is inversely related to glomerular filtration rate (GFR) and assesses renal filtration function. | |
| What is the purpose of measuring creatinine concentration? | |
| To determine kidney function, severity of kidney damage, and monitor progression of kidney | |
| disease. | |
| What is the glomerular filtration rate (GFR)? | |
| The volume of plasma filtered by the glomerulus per unit of time. | |
| What analytical method is commonly used to measure creatinine? | |
| Jaffe reaction | |
| What are some sources of error in creatinine measurement? | |
| Ascorbate, glucose, α-keto acids, and uric acids can increase measured creatinine concen | |
| tration. | |
| What is the normal reference interval for plasma creatinine in adult males using the Jaffe | |
| method? | |
| 0.9 to 1.3 mg/dL | |
| What is ammonia formed from? | |
| Deamination of amino acids during protein metabolism. | |
| What is the clinical application of measuring ammonia levels? | |
| To determine prognosis for severe liver disease and diagnose inherited deficiencies of urea | |
| cycle enzymes. | |
| What is the normal reference interval for ammonia in adults? | |
| 19 to 60 μg/dL | |
| What condition can lead to elevated ammonia levels? | |
| Severe liver disease and encephalopathy. | |
| What specimen requirements are necessary for ammonia measurement? | |
| Venous blood should be placed on wet ice immediately and centrifuged at 0 to 4°C. | |
| What is the effect of smoking on ammonia levels before collection? | |
| Patient should not smoke for several hours before collection to avoid contamination. | |
| What is the significance of elevated creatinine concentration? | |
| It indicates abnormal renal function, especially related to glomerular function. | |
| What conditions can lead to elevated creatine levels? | |
| Muscle diseases such as muscular dystrophy and trauma. | |
| What is the role of creatine phosphate? | |
| It serves as a high-energy source in muscle. | |
| What is the analytical method that improves specificity for creatinine measurement? | |
| Coupled enzymatic methods. | |
| What is the impact of bilirubin on creatinine measurement? | |
| It causes negative bias in both Jaffe and enzymatic methods. |
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