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MLT Proteins

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Question
Answer
What is a Polypeptide Chain that contains at least 59 Amino Acid Units?   Protein  
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What is the mass of a protien?   > 10,000 Daltons  
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Where are Proteins found?   In all cells of the body, fluids, secretions, and excretions  
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What are the 4 protein structures?   Primary; Secondary; Tertiary; Quaternary  
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What is the specific amino acid sequence?   Primary Structure  
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What does the winding of the polypeptide chain result in?   a Helix or Beta Pleated-Sheets  
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What is the Tertiary Structure?   The overall 3-D shape of the molecule  
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What is the Quaternary Structure?   The arrangement formed when 2 or more polypeptides join together to form a protein  
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What are the components of an amino Acid?   Amino Group; Carboxyl Group; Side Chain  
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What type of bond is formed when amino groups bind together?   Peptide Bond  
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What are the different classes of Amino acids?   Simple; Hydorxy; Sulfide; Basic; Acid; Heterocyclic; Aromatic  
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Which class of amino acids has no functional group on the side chain?   Simple amino acids  
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What are some examples of Simple Amino Acids?   Glycine, Alanine, Valine, Leucine, Isoleucine  
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Which class of amino acids has ALCOHOL as a side chain?   Hydroxy Amino Acids  
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What are som examples of Hydroxy Amino Acids?   Serine; Threonine  
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Which class of amino acids contain SULFUR as a side chain?   Sulfide Amino Acids  
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What are some examples of Sulfide Amino Acids?   Cysteine; Methionine  
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Which class of Amino Acids contains a BASIC GROUP as a side chain?   Basic Amino Acids  
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What are some examples of Basic Amino Acids?   Lysine; Arginine  
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Which class of Amino Acids contains a CARBOXYL GROUP on the side chain?   Acid Amino Acids  
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What ae some examples of Acid Amino Acids?   Aspartic Acid; Glutamic Acid  
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Which class of amino acids contains a RING GROUP (5-sided) on the side chain?   Heterocyclic Amino Acids  
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What are some examples of Heterocyclic Amino Acids?   Tryptophan; Histidine; Proline; Hydroxy Proline  
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Which class of amino acids contains an AROMATIC GROUP (6-sided) on the side chain?   Aromatic Amino Acids  
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What are the functions of protiens?   Tissue nutrition; pH buffering; Hemostasis; Transport; Biocatalyst; Immunity; Hormones  
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What is the Nitrogen content in protein?   16%; Nitrogen is not found in Carbs or Lipids  
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What is the characteristic of protein that demonstrates an absorbance in the far UV spectrum?   Absorbance Spectra  
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What is the point at which the number of (+) charged group equals the number of (-) charged group?   Isoelectric Point  
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What is the process by which a protein loses its native or original character?   Protein Denaturation  
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What are the causes of protein denaturation?   Heat; Hydrolysis via strong alkali/base; Enzymatic reaction; Precipitation by alcohol or salt; Exposure to UV; Exposure to urea or other substances  
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What is the characteristic of protein that makes it an effective antigen?   Immunogenicity  
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What two major groups are proteins classified into, based on composition?   Simple Proteins; Conjugated Proteins  
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What type of protein contains peptide chains yielding only amino acid upon hydrolysis?   Simple Protein  
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What are Conjugated Proteins composed of?   A protein (apoprotein) and a nonprotien (prosthetic group)  
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What type of protein has a metal ion attached to it?   Metalloprotein  
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What are some examples of Metalloproteins?   Ferritin (contains iron); Ceruloplasmin (contains copper); Hgb (contains iron)  
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What are Chromoproteins?   Proteins that contains an organic group for color; ex. Hgb (gives RBC color)  
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What are Lipoproteins?   When lipids such as cholesterol and triglycerides are linked together  
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What are Glycoproteins?   When carbs are joined to proteins; Molecules will be 10-40% carbs; ex. Haptoglobin  
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What are mucoproteins?   When the percentage of carbs linked to proteins is greater than 40%; ex. Mucin  
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What are proteins combined with Nucleic Acids (DNA or RNA)?   Nucleoproteins; ex. Chromatin  
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What are rare inherited disorders of amino acids metabolismdue to metabolic enzyme deficiency or Defect in amino acid transport?   Aminoacidopathies  
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Which amono acid disorder that is caused by a deficieny of Phenylalanine hydroxylase and give urine a "musty" odor"?   Phenylketonuria  
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Which amino acid disorder is caused by a decrease in Tyrosine aminotransferase?   Tyrosinemia  
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What do high levels of tyrosine lead to?   It leads to liver damage in infancy; Cirrhosis and liver cancer later in life  
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Which amino acid disorder is considered the original "inborn errors of matabolism", and also causes urine to darken upon standing due to the accumulation of homogentisic acid?   Alkaptonuria  
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Which amino acid disorder has urine, breath and skin that smells like maple syrup or burnt sugar?   Maple Syrup Urine Disease (MSUD)  
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If left untreated, which amino acid disorder causes death within one year?   Maple Syrup Urine Disease (MSUD)  
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Which amino acid disorder causes Thrombosis, Osteoporosis and dislocation of the lenses in the eye due to the lack of cystine?   Homocystinuria  
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Which amino acid disorder is caused by a defect in amino acid transport rather an enzyme deficiency?   Cystinuria  
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How much Cystein is excreted in the urine for a patient with cystinuria?   20-30 increase in urinary excretion of cystein; Its insoluble (cause urine crystals) and renal calculi  
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What is the methodology for testing Cystinuria?   Test urine for cystein using Cyanide-Nitroprusside; produces a red-purple color  
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Which amino acid disorder causes urine to have a "sweaty feet" odor?   Isovaleric Acidemia  
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Where are most proteins synthesized?   Liver  
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What does Hepatocytes do?   They secrete alpha, beta, and some gamma globulins into the circulation  
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Whaer are Immunoglobulins produced?   Plasma Cells  
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Where does disintergration to proteins occur?   Digestive tract, kidneys and the liver  
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How are amino acids excreted from the body?   amino acids are deaminated producing ammonia, which is then converted to urea and excreted in the urine  
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What is the breakdown of complex molecules into simpler ones for energy production, recycling or excretion?   Catabolism  
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What is Anabolism (constructive metabolism)?   building up of complex molecules  
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What is the balance between anabolism and catabolism?   Nitrogen Balance  
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What is Positive Nitrogen Balance?   When Anabolism > Catabolism  
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What is Negative Nitrogen Balance, and when does it occur?   Catabolism > Anabolism; Occurs during Burns, starvation and wasting tissues  
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Which plasma protein migrates ahead of albumin during electrophoresis?   Prealbumin  
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Whish plasma protein has the highest concentration in the serum?   Albumin  
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Which plasma proteins maintains of osmotic pressure and binds various substances in the blood?   Albumin  
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What is the absence of albumin?   Analbuminemia  
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When would you see a decrease in serum albumin levels?   Severe malnutrition; Inadequate source of amino acids; liver disease; GI loss; Loss in urine due to renal disease  
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If a patient is dehydrated would their albumin levels be Increased or decreased?   Increased  
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Which plasma protein accounts for 90% of the fraction of serum proteins that migrates electrophoretically immediately following albumin?   Alpha-1-antitrypsin  
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Where is Alpha-Fetoprotein (AFP) synthesized?   Synthesized by the fetus (synthesized by teh fetal yolk sac, then by the parenchymal cells of the liver  
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When does AFP increase?   during pregnany; Increases in the presence of twins; Spina Bifida; Neural tube defects  
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What would indicate an increased risk for Down's Syndrome?   Decreased levels of AFP  
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Why does AFP increase during pregnancy?   Due to the AFP crossing the palcenta  
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Which plasma protein is composed of 5 carb units attached to a polypeptide chain?   Alpha-1-Acid Glycoprotein (Orosomucoid)  
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When would you see increased levels of Alpha-1-Acid Glycoprotein?   Pregnancy, Cancer and diseases associated with cellular proliferation  
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What is a chemical complex of lipids and proteins synthesized in the liver, consisting of HDL?   Alpha-1-Lipoproteins  
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What plasma protein is composed of 2 alpha and 1 beta chain polypeptides?   Haptaglobin (aka alpha-2-glycoprotein)  
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When are increased levels of Haptaglobin seen?   Increased levels are seen in inflammationburns, therefore suited for evaluation of rheumatic diseases  
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What is a copper containing metallo-protein that has enzyme activities?   Ceruloplasmin (Ferroxidase)  
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Which plasma protein consist of LDL (contains cholesterol) and VLDL (contains triglycerides)?   Beta-Lipoprotein  
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Which plasma protein has 2 transferrin ions bound to each molecule?   Transferin  
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What are the major functions of Transferrin?   Transport iron and prevent iron loss through the kidneys  
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In what conditions would you see an increase in transferrin levels?   Hypochromic and Microcytic Anemia  
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What is one of the largest plasma proteins synthesized in the liver, that is considered a glycoprotein due to ist carb content?   Fibrinogen  
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What plasma protein is stimulated by an immune response to foreign particles and microorganisms?   Immunoglobulins  
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What is the purpose of Total Protein (TP) testing?   To detect abnormalities in the total serum protein levels  
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Which protein testing methodology is based for nitrogen deamination ansd is very precise and accurate?   Kjeldahl Method  
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Why is the Kjeldahl Method not used much?   It is too time consuming  
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which protein testing method is used with spectrophotometry and is related to the UV absorbance of polypeptide bonds?   BIURET Method  
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What are the specimen requirements for protein testing?   Use serum, and sample must be clear and stable for 1 week at 25 degrees Celsius  
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What is the methodology for albumin testing and what is the dye of choice?   Dye-binding method; Dye of choice is Bromcresol Green  
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When would a patien experience hyperalbuminemia?   when dehydrated  
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