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chemistry amino acid
| Question | Answer |
|---|---|
| What is prealbumin? | Migrates ahead of albumin, transports with throid hormones and retinal. |
| Albumin | Highest concentration 40-60%. Responsible for oncotic pressure. Strong negative charge. |
| cotic pressure | Force that confines fluids within the vascular compartment. |
| Analbumemina | Total absence of albumin |
| Globulins | Alpha 1,2, Beta and gamma globulins |
| Antitrypsin | Main function to inhibit lysosomal elastase and chymotrypsin |
| AAT | Antitrypsin |
| Fetoprotein | AFP/ glycoprotein normally present in low concentrations. Peaks in fetus 13 weeks and recedes by 34th week.Diagnosis for neural tube defects, fetal blood loss. |
| Decreased amount of AFP | associated with down syndrome |
| Glycoproteins | mucoprotein composed of five carbs attached to peptide chaininhibits phagocytic activity and platelet aggregation |
| AGP | Glycoproteins |
| Haptoglobin | HP |
| Primary function to bind free hemoglobin | Haptoglobin (HP) |
| Cerloplasmin | Cer |
| Cerloplasmin | copper oxidase enzyem, single polypeptide, regulate iron transport and utilization |
| Macroglogulin | Largest plasma protein, functions as a protease inhibitor by blocking the active site on enzymes such as plasmin, thrombin |
| A2M | Macroglogulin |
| What are the Beta Globulins | Transferrin, Beta 2 Macroglobulins, Fibrinogen, complement, c-reactive protein |
| transferrin | major function is to transport oxidized ions of iron. Major component of beta globulins in body. |
| Alpha 2 Macroglogulin | largest plasma protein,protease inhibitor by blocking the active site on enzymes such as plasmin |
| What beta globulin is useful in assessing renal function | Macroglobins |
| What Beta 2 globulin is useful in monitoring multiple myloma and b cell tumors? | Macroglobulin |
| Fibrinogen | Beta globulin activated by thrombin to form fibrin by cleaving fibrinopeptides from the fibringens chain to form a fibrin clot. |
| Complement | Beta Globulins, 25 proteins sequential manner. |
| Causes lysis, opsonize cellular debris prior to phagocytosis mediate inflammatory response | Complement |
| What protein has the highest concentration in complement? | C3 |
| C-reactive | Beta globulins, bind c-polysaccaride on the cell wall of s.pneumonia |
| what is the major function of C-reactive protein? | C-reactive form complexes with microorganism to faciliate activation of classical pathway. |
| What beta globulin initiates opsonization, phagocytosis and lysis of foreighn cell in complemant pathway | C-reactive (CRP) |
| Immunoglobulins | synthesized by plasma cells stimulated by immune response to foreighn particle |
| what are the 5 major groups of immunoglubulins | IgG, IgM, IgA, IgE,IgD |
| What is a Kappa and Lambda? | light chain |
| The differences in a heavy chain are called? | Idiotypes |
| Monoclonal immunoglobulin | a molecule or immunoglobulin that is derived from the proliferation of one plasm cell |
| IgG | most abundant75% long term physiological protection neatralizing bacter or viral antigens |
| IgA | two subtypes dimeric secretory |
| IgM | first antibody to appear due to antigenic stimulation, largest in size, surface of b-cells |
| IgD | surface of b lymphs, function unknown |
| IgE | lowest conc, associated with allergic reactions, rapidly attach to mast cells |
| Myoglobulin | heme protein found in striated skeletal and cardiac muscles |
| What can reversible bind oxygen | myoglobulin |
| If myologlubin is elimated what does is cause? | kidney damage |
| troponin | regulate muscle contractions |
| Used to assess the risk of patients with acute myocardial ischemia | Tropinin T |
| Fibronectin | identical subunits, cell adhesion, tissue differentiation, growth and wound healing |
| used as a predictor of preterm labor | fibronectin |
| Inborn errors of metabolism, rare | amino acidopathies |
| Phenylketouria | Amino acidopathies, PKU, absence of PKA, buildup of phenylpyruvate, heel prick |
| disorder of tyrosine transaminase | Tyrosinemia(amino acidopathies) buildup of of Tyrosine |
| Urine darkening upon standing | Amino acidopathies/ Alkaptonuria/first error discovered/ |
| Homocystinuria | Amino aciopathies/formation of cystine, impaired enzyme, def.folic acid, vita b6 and b12 |
| specimens use dfor amino acid testing | urine and blood |
| composed of carbon, oxygen, sulfur, nitrogen | proteins |
| functions of proteins | oncontic pressure, tranportation, hormones, buffer |
| hypoproteinemia | protein levle less than reference range, cause by excessive plasma protein loss, decrease in protein intake |
| results of hypoproteinemia | def.in essential amino acids, impaired protein syntheses seen in liver disease inheristed immunodeficiency disorders |
| Hyperproteinemia | protein levels greater than reference range |
| what can cause dehydration | hyperproteinemia |
| multiple myeloma | hyperproduction of IgG, neoplastic cells proliferate in the bone marrow |
| M spike | multiple myeloma |
| waldenstroms macroglobulinemia | monoclonal paraprotein of IgM type |
| symptons of waldenstrom? | fewer bact. infections, less bone pain, thick serum due to IgM |
| what are the five total protein tests | Kjeldahl, refractometery, biuret, dye binding, protein fractionation |
| classic method of total proteins | kjeldahl |
| Tungtstic acid to precipitate proteins | kjeldahl |
| measure the refraction of the serum vs water for total proteins, what is the test? | Refractometry |
| quick method of determining the protein volume | refractometry |
| biuret | cupric ions combining with the peptide bonds in an alkaline pH, forms violet color, measured spectrophotomically at 540nm |
| Total Protein-Dye binding | most proteins have affinity for dyes and will bind |
| Most common dyes used for dye binding | bromphenol blue, ponceau S, Coomassie brillant blue 250 |
| What test measures the dye absorption by spectrophotometry as a shift in absorbance at 465-595 nm? | Dye binding |
| total protein fractionation | used wheneleof protein is found, testing for further seperae the 5 fractions is done by electrophoresis |
| what are the the three alpha 1 globulins? | Antitrypsin(AAT), fetoprotein(AFP), Glycoproteins(AGP) |
| What are the Alpha 2 globulins | Haptoglobin(Hp), Ceruloplasmin(Cer), Macroglobulin(A2M0, |
| What are the Beta Globulins? | Transferrin(TRN), Macroglobulins, Fibrinogen |
| Trn | transferrin |
| AFP | Fetoprotein |
| AGP | Glycoproteins |
| Hp | Haptoglobin |
| Cer | Ceruloplasmin |
| A2M | Macroglogulin |
| Salt fractionation | globulins are seperated from albumin by precipitating them out using salt |
| what is the name of the test that allows binding of anionic dye? | Dye binding Albumin |
| What type of dye has a different absorbtion than free dye? | bound dye |
| Direct colorimetric measurement | Globulin test method, glyxylic acid is the presence of cupric ions and an acid medium produce a purple color. |
| How do you determine albumin levels? | subtract total protein levels from total glubulin levels |
| what test is not commonly used for globulin testing? | Direct colorimeric measurement |
| Tumor marker for hepatomas | Fetoprotein |
| Primary clinical use is iron saturation | Transferrin |
| Total iron binding capacity used which beta globulin? | transferrin |
| Name the 5 diseases accociated with amino acidopathies? | Phenylketouria, tyrosemia,alkaptonura,maple syrupe disease and homocystinuria |
| disorder of homogenistic acid oxidase | Alkaptonuria |
| disorder of tyrosine transaminase | tyrosinemia |
| Urine smelss like maple syrup,heriditary | maple syrup disease |
| where does protein synthesis begin | liver |
| how are proteins classified | simple and conjugated |
| total nitrogen | measures all chemically bound nitrogen within samples. |
| what gives a false negative in total nitrogen test | urea and creatine |
| how is total nitrogen measured | chemilluminescence, sample heated in the presence of oxygen, nitric oxide forms/excited nitrogen dioxide molecule (NO2) |
| Kjeldahl | nitrogen converted to ammonium borate which is measured thru titration with HCL |
| Total protein fractionation | used when elevation of total protein is found, testing to further seperate the 5 fractions is done by electrophoresis |
| total protein dye binding | dye absorbtion is measured spectrophotomically as a shift in absorbance at 465 to 595 nm |
| Total protein dye binding | used to stain bands after electrophoresis |
| serum protein electrophoresis | standard method involves sample appplied to the neg.charge in an alkaline buffer of 8.6. |
| Proteins are seperated based on strength of the charge/divides in 5 bands | serum protein electrophoresis |
| protein analysis | high resolution protein electrophoresis,higher voltage conc,buffer |
| capillary electroph |
Created by:
joanndibattisto
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