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