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Chem 2 Ch.10

Amino Acids and Proteins

TermDefinition
Amino Acids -building blocks of proteins
Peptide bond amino acids joining together
Aminoacidopathies class of inherited errors of metabolism in which there is an enzyme defect that inhibits the body's ability to metabolize certain amino acids
Phenylketonuira Absence of activity of the enzyme phenylalanine hydroxylase
Tyrosinemia -Inborn metabolic disorders -characterized by the excretion of tyrosine and tyrosine catabolites in the urine. -5 different enzymes that are needed to break down tyrosine
Alkaptonuria -transmitted as an autosomal recessive gene ( HGD), which causes the lack of the enzyme homogentisate oxidase which is needed in the metabolism of tyrosine and phenylalanine.
Maple Syrup Urine Disease -absence or greatly reduced activity of the enzyme branched-chain a-ketoacid decarboxylase -blocks the normal metabolism of the three essential branched-chain amino acids leucine, isolucine and valine. - autosomal recessive genetic inherited disorder.
Isovaleric Acidemia -autosomal recessive metabolic disorder from a deficiency of the enzyme isovaleryl-CoA dehydrogenase -prevents normal metabolism of the branched-chain amino acid leucine
Homocystinuria lack of the enzyme cystathionine-B synthetase -necessary for the metabolism of the amino acid methionine
Cystinuria -defect in the amino acid transport system. -inadequate reabsorption of cystine during the filtering process in the kidneys.
Primary Structure # and types of amino acids in the sequence
Secondary Structure repeating structures stabilized by hydrogen bonds between the amino acids within the protein. ( Pleated sheet or helix)
Tertiary Structure overall shape ( fold)
Quaternary Structure shape or structure that results from the interaction of more than one protein molecule. (3D)
Denaturation loss of its native structure.
Proteinuria
Simple proteins -contain peptide chains composed of only amino acids. -globular or fibrous
Conjugated Proteins -consist of a protein and a nonprotein (prosthetic) group -the prosthetic groups could be lipid, carb, porphyrins & metals -something is JOINED to it
Globulins a1-Globulns a2-Globulins Haptoglobulins B-globulins
Alpha 1-Antitrypsin (AAT) -glycoprotein mainly synthesized in the lover - most important function inhibition of the protease neutrophil elastase.
Alpha1- Fetaprotein -synthesized in the developing embryo and fetus and than by parenchymal cells of the liver.
Haptoglobin -a2-glycoprotein synthesized in the hepatocytes. -elevated in many inflammatory diseases
Transferrin -glycoprotein -negative acute-phase protein -synthesized in liver
Siderophilin transferrin
Lipoproteins -complexes of proteins and lipids -transport cholesterol, triglycerides & phospholipids in blood
B2-Microglobulin -histocompatibility complex -present in high concentrations on lymphocytes
Complement one of the natural defense mechanisms that protects the human body from infections. -synthesized in the liver as single polypeptide chains and circulate blood as nonfunctional precursors.
Fibrinogen -one of the largest proteins in blood plasma -synthesized in liver
C-Reactive Protein -one of the first acute-phase proteins to rise in response to inflammatory disease.
Immunoglobulins -IgG is most abundant -IgG crosses placenta -antibodies produced by the B lymphocyte that confer humoral immunity.
Myoglobin -153 amino acids -primary oxygen-carrying protein -muscle protein -toxic to the kidneys and kidneys can be damaged
Troponin -"gold standard"
Brain Natriuretic Peptide -popular marker for congestive heart failure -found in left ventricle myocardium
Cystatin C -low molecular mass protein -120 amino acids -marker for early assessment of changes to the glomerulus filtration rate
Hypoproteinemia Low total protein and occurs in any condition where a negative nitrogen balance exists.
Hyperproteinemia increase in total plasma proteins, not a disease state but underlying cause of dehydration
Growth,repair and maintenance of all cells are dependent on? Amino acids
Amino acids contains? ( basic structure) at least one of both amino and carboxylic acid functional groups
(-NH2) and ( -COOH ) bond to the a-carbon with the amino group of one amino acid linking with the carboxyl group peptide bond
catalyzes the conversion of phenylalanine to tyrosine Phenylalanine hydroxylase
Type 1 tyrosinemia -most severe 1 in 100,000 births -caused by low levels of the enzyme fumarylacetoacetate hydrolase
Type 2 tyrosinemia -caused by a deficiency of the enzyme tyrosine aminotransferase
Type 3 tyrosinemia -rare disorder -caused by a deficiency of the enzyme 4-hydroxyphenylpyruvate dioxygenase.
Urine turns brownish-black when mixes with air ( aminocidopathy) Alkaptonuria
sweaty feet odor Isovaleric Acidemia
Cause of a1-Antitrypsin Mutations in the SERPINA1 gene
Protein used to evaluate the rheumatic diseases and increased in burns and nephrotic syndrome Haptoglobin
Functions of transferrin transport of iron and the prevention of loss of iron through the kidney
low transferrin levels -impaired hemoglobin production and lead to anemia. -due to poor production of transferrin as seen in liver disease or malnutrition or excessive loss of transferrin through the kidneys into the urine.
increased transferrin levels iron deficient anemia
low prealbumin levels hepatic damage, acute phase inflammatory response and tissue necrosis. -poor nutrition
increased prealbumin levels patients receiving steroids, in alcoholism and in chronic renal failure.
low albumin levels malnutrition, liver disease, hypothyroidism, dilution by excess, acute disease states, redistribution
high albumin levels seen ONLY with dehydration or after excessive albumin infusion
decreased levels of ceruloplasmin wilsons disease
increases levels of ceruloplasmin inflammation, severe infection & tissue damage
elevated serum levels of B2-Microglobulin impaired clearance by the kidney or overproduction of the protein that occurs in inflammatory diseases.
increased complement inflammatory states
decreased complement malnutrition and hemolytic anemia.
most abundant complement protein in human serum C3
decreased levels of C3 autoimmune disease, neonatal respiratory distress syndrome, bacteremia, tissue injury and chronic hepatitis.
increased fibrinogen levels inflammatory, pregnancy and use of oral contraceptives
decreased fibrinogen reflect extensive coagulation
increased C-Reactive protein acute rheumatic fever, bacterial infections, myocardial infarctions, rheumatoid arthritis, carcinomatosis, gout and viral infections
% of protein composition in immunoglobulins 82%-96%
% of carbohydrate composition in immunoglobulins 4%-18%
increased IgG liver disease, infections, IgG myeloma, parasitic disease and many rheumatic diseases
decreased IgG acquired immunodeficiency, protein-losing states and non-IgG myeloma
Increased IgA liver disease, infections and autoimmune diseases
decreased IgA depressed protein synthesis and immunodeficiency
Increased IgM toxoplasmosis, primary biiary cirrhosis, cytomegalovirus, rubella, herpes, syphilis and various bacterial and fungal diseases.
decreased IgM protein-losing conditions and hereditary immunodeficiency
Increased IgD infections, liver disease and connective tissue disorders
Increased IgE infectious diseases, asthma, hay fever & IgE myeloma
increased myoglobin levels progressive muscular dystrophy & crushing injury in which skeletal muscle is damaged. & renal failure
increased troponin levels heart injury is present or that the injury took place more than 24 hours in the past.
most common test methods for testing proteins Biuret and Die Binding
what test used copper ions that caused a deep blue color during total protein analysis Biuret
Diseases associated with alterations in cerebrospinal fluid proteins Bacterial, viral and fungal meningitis; traumatic tap; multiple sclerosis; obstruction; neoplasm; disk herniation & cerebral infarcation
a1-Antitrypsin Deficiency on elecrophoresis normal albumin, decrease a1 fraction
Monoclonal Increase on elecrophoresis Increased gamma globulin
Nephrotic Syndrome on electrophoresis Decreased Albumin, Increased a2 and Beta globulins
Inflammation on electrophoresis Increased a1, a2 and beta globulins
Cirrhosis on electrophoresis Beta & Gamma Bridge
Order of fractions on electrophoresis Albumin, a1, a2, beta than gamma
Reference range for Total Protein 65-83 g/L
Reference range for Albumin 35-55 g/L
Created by: Sdevries0982