proteins – Chemistry Test Answers – Flashcards
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| Nucleoside |
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| purine or pyrimidine covalently bonded to a sugar |
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| Nucleotide |
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| nucleoside to which 1-3 phosphate groups are covalently bonded |
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| Nucleic Acids |
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| Polymer of nucleotides covalently liked by phosphodiester bonds |
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| Deoxyribonucleic Acid |
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| (DNA) double stranded nucleic acid composed of repeating nucleotides |
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| Ribonucleic Acid |
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| (RNA) Single stranded nuclein acid found in every living cell. |
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| Gene |
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| single stranded section of DNA that codes for proteins |
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| Chromosome |
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| liner, double stranded, carry all of an organisms genetic information. |
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| Metabolism |
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| the sum of all biochemical reactions that occur within a cell. |
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| Chemical Components of Nucleotides |
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| * Pentose Sugar * 1-3 Phosphate Groups * Nitrogenoous base |
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| Components of DNA |
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| Nitrogenous Bases: Adenine, Guanine Thymine & Cytosine Pentose Sugar - Deoxyribose Phosphate Groups |
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| Mutation |
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| a change in the DNA base sequence in a gene. can result from substitutions, insertions or deletions. |
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| How can mutations affect a protein? |
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| 1) No effect 2) Diminished or complete loss of protein function. 3) Creation of a new function |
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| Components of RNA |
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| Nitrogenous bases: Adenine, Guanine, Uracil, Cytosine Pentose sugar - Ribose Phosphate Groups |
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| Structure of RNA |
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| single stranded complementary paired bases: Adenine - Uracil Guanine - Cytosine |
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| Messenger RNA (mRNA) |
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| carries genetic information for a protein from DNA to the ribosomes |
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| Ribsomal RNA (rRNA) |
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| the "platforms" where protein synthesis occurs. |
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| Transfer RNA (tRNA) |
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| delivers the correct amino acid to the ribosome to be incorporated into a new protein |
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| Transcription |
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| DNA->RNA The process in which a gene is a template for the creating of RNA. Occurs in the cell nucleus |
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| Translation |
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| mRNA->Protein the process where mRNA is used to create a protein. Occurs in cytolplasm on ribosomes. |
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| Codon |
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| The three base sequences that encode a single amino acid |
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| Replication |
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| process by which DNA is copied, basis for biological inheritance. Occurs in the nucleus. |
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| Protein |
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| polymer of amino acids covalently joined by peptide bonds. |
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| Peptide Bond |
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| Covalent bond between the carboxyl group of one amino acid and the amino group on another. |
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| Zwitterion |
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| ion that has both a positive and a negative charge. formed as the amino group is protonated and the carboxyl group is dissociated. |
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| Denaturation |
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| the organized structure of a protein is disrupted. Results in loss of function. |
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| Acute Phase Reactants (APR) |
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| proteins whose concentrations change after trauma, burns, etc. |
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| Cryoglobulin |
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| precipitate or gel whens erum is cooled, but re dissove when it is warmed. |
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| Immunoglobulins |
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| antibodies |
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| Elements contained in all proteins |
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| Carbon, Hydrogen, Oxygen, Nitrogen |
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| R-Group |
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| hydrophobic or hydrophillic, a variable group of atoms attatched to every amino acid. |
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| Primary Structure of Proteins |
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| linear sequence of amino acids, held together by polypeptide bonds. |
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| Secondary Structure |
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| folding of the primary structure. cause principally by hydrogen bonds. |
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| Tertiary Structure |
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| additonal folding of the secondary structure, places hydrophobic AA on the inside and hydrophillic on the outside. |
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| Quaternary Structure |
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| overall 3-D folding of 2 or more polypeptides. |
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| Globular Protein |
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| compact, spherical structures, generably soluble in salt, most proteins in body. I.E. albumin, antibodies, enzymes, hormones, and hemoglobin. |
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| Fibrous Proteins |
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| relatively long, generably insoluable in salt, represent structural protiens, I.E. Collagen, Elastin, Keratin, Actin, Myosin |
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| Functions of Proteins |
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| 1) Antibodies 2) Catalyze biochemical reactions 3) Transport molecules 4) regulatory roles 5) structure 6) movement 7) nutrients |
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| Hemoglobin |
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| oxygen carrying protein found in RBCs, contains 4 heme groups and 4 polypeptides. |
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| Functions of Hb |
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| Gas Transport Acid Base Balance |
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| Components of Hb |
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| Heme Globin |
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| Heme |
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| Protoporphyrin IX ring, and Ferrous Ion |
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| Site of Heme Synthesis |
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| Bone Marrow. |
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| Aminoeleluniv acid (ALA) Synthase |
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| catalyzes the initial step, heme inhibits this enzyme. |
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| Lead Inhibition |
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| inhibits all steps in porphyrin synthesis by denaturation |
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| Myoglobin |
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| found in muscle tissue, reserve supply of O2. contains one polypeptide and one protoporphyrin ring. |
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| What are the factors affecting Oxygen Transport? |
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| Partial PRessure of Oxygen, PH, Temperature, 2,3-DPG |
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| How does decreased P50 affect O transport? |
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| shift to the left, and an impaired oxygen release to tissues |
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| How does an increased P50 affect O transport? |
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| shift to the right, eases the delivery of oxygen to tissues. |
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| How does Increasded blood acidity affect O transport? |
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| decrease PH, shift to the right, lowering of affinity for O2 |
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| How does decreased blood acidity afftect O transport? |
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| increased PH, shift to the left, increase affinity for O2 |
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| How does temp increase affect O transport? |
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| hemoglobin more readily releases O2, shift to the right. |
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| How does temp decrease affect O transport? |
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| hemoglobin less readily releases O2, shift to the left. |
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| 2,3-DPG is significant because? |
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| essential in enabling the unload of O2 and it is the most important factor that affects O2 transport. |
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| What are the 4 forms of normal Hemoglobin? |
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1) Normal Hb A 2) Normal Variant Hb A2 3) Normal Variant Hb A1c 4) Fetal Hb F |
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| Why is Hb A1c Significant? |
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| the concentrations serve as an indicator for prolonged high glucose concentrations, used to monitor diabetics |
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| Bilirubin |
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| the breakdown product of the normal heme catabolism. |
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| What happens to Iron during heme catabolism? |
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| iron is recycled, by being released from the heme and then returned to the plasma, then it is carried to the bone marrow. |
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| What are the factors that denature proteins? |
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| Heat, organic solvents (Alcohol), Detergents, salting out, pH changes, HEavy metals, mechanical stress |
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| How does heat denature proteins? |
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| as temp increases, molecular motion inceases, bonds are disrupted. |
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| Simple Proteins |
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| yield only amino acids when hydrolyzed. I.E. albumin, insulin, fibrinogen. |
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| Conjugated Proteins |
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| yield amino acids, and a non protein substance upon hydrolysis |
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| Glycoproteins |
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| covalently linked carbohydrate |
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| Phosphoproteins |
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| covalently linked phosphate groups |
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| Lipoproteins |
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| covalently linked lipids, like cholesterol, triglyceride, and phospholipids. |
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| Metalloproteins |
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| contain ions and are often colored. I.E. chlorophyll and hemoglobin |
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| Essential Amino Acids |
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| isoleucin, leucin, lysine, methionine, phenylalanine, threonine, tryptophan, and valine |
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| Liver uses amino acids, for: |
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| Growth, maitenence, repair, enzyme production, albumin, lipoproteins. |
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| Where are immunoglobulins produced? |
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| B lymphocytes that originate in bone marrow |
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| Where are plasma proteins synthesized? |
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| in the liver, circulate the blood stream. |
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| Prealbumin |
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| Tryptophan rich tetrameric glycoprotein, mainly synthesized in the liver. |
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| Prealbumin Function |
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| Carrier for thyroid hormones, and Vitamin A. Used to assess the patients nutritional state. |
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| Clinical Significance of Prealbumin |
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| decreases in liver disease, increases with steroid use, pregnancy and chronic renal disease. |
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| Antibody |
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| immunoglobulins. produced in response to an antigen. |
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| Antigen |
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| substance that stimulates antibody formation |
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| Phenylketonuria (PKU) |
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| genetic deficiency of the enzyme phenylalanine hydroxylase |
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| Maple Syrup Urine Disease (MSUD) |
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| genetic deficiency in the enzyme that degrades the branched chain amino acids; branched chain alpha ketoacid dehydrogenase |
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| Causes of Hypoproteinemia |
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| Causes of Hyperproteinemia |
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| Porphyrin Conditions |
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Porphyrinuria - excessive excretion in urine Porphyrinemia - presence of porphyrin in the plasma or serum |
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| Porphyrin Disorders |
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Hereditary - genetic disorders from impaired activeity of enzymes Acquired - more common; lead poisoning, renal failure, iron deficiency, liver disease |
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| Photoporphyrias |
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| cutaneous porphyria that presents itself with exposure to light. |
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| Thalassemias |
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| disease state from globin genetic mutations that result in little globin protein being produced. It affects Hbs O transport. |
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| Sickle Cell Anemia |
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Hb S sickled RBC, most common type of abnormal Hemoglobin, results from single mutation of the B globin. can be life threatening. |
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| Carbaminohemoglobin (CO2Hb) |
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| compound of CO2 and Hb. about 10-20% of co2 binds to globin, forming this. |
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| Methemoglobin (M-Hb) |
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| hemoglobin where the iron molecule is oxidized to Fe+3 which cannot bind oxygen. |
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Sulfhemoglobin (S-Hb)
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green pigmented compund of hydrogen sulfide and Hb. irreversible oxidation, sometimes after exposer to TNT, or sulfur. |
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| Carboxyhemoglobin (COHb) |
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formed by the binding of CO to heme. normally .2-.8% smokers up to 10%. Co poisoning exhibits cherry red color. |
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| Cryoglobulin Clinical Significance |
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| seem in myeloma, macroglobulinemia, autoimmune diseases like, rheumatoid arthritis, & SLE |
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| Functions of Immunoglobulins |
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| 5 classes of Immunoglobulins |
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| IgG, IgM, IgA, IgD, IgE |
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| Multiple Myeloma |
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| malignant diseases caused by the presence of neoplastic plasma in bone and bone marrow |
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| How are Bence-Jones Proteins analyzed? |
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Heating urine to 40-60C, they will precipitate while others remain in solution. at 100C proteins will redissolve. Cooling reverses this. |
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| C-reactive Protein (CRP) |
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| APR, most sensitve indicator of inflammation, rises about 8 hours after onset, increases in all bacterial infections, rarely with viral |
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| Haptoglobin |
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| APR concentrations increase in hypoalbuminemia states like nephrotic syndrome. |
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| Ceruloplasmin |
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| APR carries 90% of the copper in plasma |
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| Alpha1-antitrypsin |
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| may protect the body from proteolysis by proteases released from leukocytes and macrophages. |
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| Alpha2-macroglobulin |
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| Protease inhibitor |
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| Fribinogen |
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| Essential blood clotting protein |
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| C3/C4 |
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| Early components of the complement system |
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| Transferrin |
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| transport protein for iron. decrease seen in inflammatory response |
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| Albumin |
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| Levels may decrease to divert protein production away from the liver and towards the components increasing for inflammatory response |
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| Prealbumin |
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| Decrease related to protein malnutrition |
