Amino Acids & Proteins

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1

acute phase reactions

when both major α₁ proteins (α₁-antitrypsin and α₁-glycoprotein), α₂-band proteins (ceruloplasmin and haptoglobin), β-globulins, C3, C4, and C-reactive protein are increased and albumin is decreased

2

α₁-acid glycoprotein (AAG)

major glycoprotein that increases during inflammation; elevated levels are found in rheumatiod arthritis, cancer, pneumonia, and other conditions

3

α₁-antichymotrypsin (ACT)

serine proteinase that catalyzes chymotrypsin and mast cell chymase

4

α₁-antitrypsin (AAT)

major α₁-globulin making up approximately 90% of α₁-proteins; a glycoprotein, serum trypsin inhibitor, and acute phase reactant with antiprotease activity; deficiency of AAT results in emphysema or chronic obstructive pulmonary disease in adults and cirrhosis in adults or children

5

α₂-macroglobulin (AMG)

one of the largest plasma proteins; involved in primary or secondary inhibition of enzymes in the complement, coagulation,and fibrinolytic pathways

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albumin/globulin (A/G) ratio

ratio of albumin to globulin proteins in the serum; reference range for ration is approximately 1.0-1.8, with albumin levels normally higher than globulins

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albumin

synthesized in liver; makes up approximately 60% of total serum protein; chief biological function is to maintain plasma colloidal osmotic pressure

8

alkaptonuria

a rare inherited disease that results from the deficiency of the enzyme homogentisic acid oxidase in the catabolic pathway of tyrosine; deficiency leads to buildup of homogentisic acid in the tissues of the body

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alpha-fetoprotein

principal fetal protein (fetal albumin-like protein) in maternal serum used to screen for the antenatal diagnosis of neural tube defects, including spina bifida and anencephaly

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amino acids

molecule containing amino group (NH₂), carboxyl group (COOH), hydrogen, and R group (radical or side chain) with formula RCH(NH₂)COOH

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ampholyte

when both COOH and NH₂ groups on amino acid become ionized NH₃+

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amphoteric

containing two ionizable sites; proton-accepting group (NH₂) and proton-donating group (COOH)

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analbuminemia

absence of albumin, a genetic autosomal recessive trait

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anencephaly

congenital absence of the brain and cranial vault; condition is incompatible with life

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apoprotein

conjugated proteins without their nonprotein groups or ligands

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β₂-microglobulin

low-molecular-weight protein on cell membrane of most nucleated cells; found in especially high levels in lymphocytes; makes up common light chain of class I major histocompatibility complex antigens found in all nucleated cells

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biuret reaction

commonly used protein methodology that occurs when solution of protein is treated with cupric divalent ions in moderately alkaline medium and forms violet-colored chelate that absorbs light at 540 nm; peptide bond forms between cupric ion and carbonyl oxygen and amide nitrogen atoms of peptide bond

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bromcresol green

anionic dye of triphenylmethane family with four bromine atoms that binds to albumin and is common albumin methodology

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bromcresol purple

anionic dye with two bromine atoms that binds to albumin and is common albumin methodology

20

ceruloplasmin (Cp)

principal copper-containing protein in plasma, comprising 95% of the total serum copper; primary role seems to be in plasma redox reactions, where it can be an oxidant or antioxidant, depending on various factors such as presence of ferric ions and ferritin binding sites; serum levels increase in Wilson disease

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conjugated protein

proteins that have nonprotein groups attached to them that provide certain characteristics to protein (e.g. lipoproteins)

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c-reactive protein

acute phase reactant and nonspecific indicator of bacterial or viral infection, inflammation, and tissue injury or necorsis

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cystinuria

hereditary disease characterized by excretion of large amounts of cystine, arginine, ornithine, and lysine in urine that leads to development of cystine calculi

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denaturation

separation of double-stranded DNA molecule into two single stands by treatment that disrupts hydrogen bonds between strands; disruption of bonds holding secondary, tertiary, or quaternary structures of protein, resulting in loss of activity and also functional and structural characteristics

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essential amino acids

amino acid not synthesized by body that must be ingested in diet; in humans, 8 to 10 essential amino acids (valine, leucine, isoleucine, phenylalanine, tryptophan, methionine, threonine, and lysine) required by adults; infants require two additional amino acids (arginine and histidine)

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fusion of the β-γ bands (bridging)

common abnormal protein electrophoresis pattern that results from fast moving γ-globulins that prevent resolution of β- and γ-globulins; cirrhosis is most common cause of β-γ bridging

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γ-globulins (IgG)

immunoglobulin or humoral antibody; IgG antibodies are produced in response to antigens of most bacteria viruses

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globular protein

compact, folded, and coiled protein chains that are relatively stable

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globulin

group of proteins that make up approximately 38% of total protein in serum; help to control plasma osmotic pressure in capillaries, have an important role in body's immune response, and serve as carrier proteins for various substances in plasma

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glycoprotein

compounds consisting of simple protein and carbohydrates, which make up less than 4% of total weight

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haptoglobin

an α₂-globulin, mucoprotein, and acute phase reactant that binds free hemoglobin in plasma; increases inflammatory conditions and decreases in hemolytic disorders

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hemopexin

protein that removes heme from circulation; when red blood cells are destroyed, hemopexin transports heme to liver, where it is catabolized by reticuloendothelial system

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homogentisic acid

product of autosomal recessive condition and alkaptonuria

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hyperalbuminemia

condition associated with increase in albumin, which is usually artifactual; relative hypoalbuminemia due to decrease in plasma volume

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hyperproteinemia

condition associated with positive nitrogen balance; dietary nitrogen intake is greater than excretion or loss of nitrogen, which occurs mainly in urine; usually associated with hemoconcentation or dehydration, resulting in decreased plasma volume

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hypoalbuminemia

decreased albumin levels with most common cause being increased catabolism because of tissue damage and inflammation; found in people who are malnurished and individuals with chronic liver, kidney, and pancreatic disease

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hypoproteinemia

decreased levels of protein in the blood; condition related to negative nitrogen balance or when excretion of nitrogen exceeds intake or synthesis of protein; most common cause is increase plasma water volume or hemodilution, which results in decrease in concentration of all proteins

38

immunoglobulin (Igs)

plasma polypeptides that bind with antigenic proteins and serve as one of body's defenses against disease; comprise two heavy chains and two light chains; five types

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immunoglobulin A (IgA)

molecular weight 160,000; 10-15% of Igs

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immunoglobulin D (IgD)

molecular weight 184,000; <1% of serum Igs

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immunoglobulin E (IgE)

molecular weight 180,000; extremely low concentrations (0.µg/mg)

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immunoglobulin M (IgM)

largest Ig (molecular weight 900,000); 5-10% of total Igs

43

isoelectric point (pl)

hydrogen-ion concentration (pH) at which amino acid or protein has no net charge and positive charges equal negative charges

44

lipoprotein

lipoprotein particle that resembles LDL with addition of carbohydrate rich protein apo (a) that is bound to apo B-100, with each molecule containing one molecule of apo (a) and one molecule of apo B-100; contributes to obstruction of blood vessels in atherosclerosis

45

maple syrup disease (MSUD)

genetic disorder named for characteristic maple syrup or burnt sugar odor of affected individual's urine; caused by absence of or extremely low levels of α-ketoacid decarboxylase enzyme, which results in abnormal metabolism of three essential amino acids: leucine, isoleucine, and valine

46

metalloprotein

proteins that have metal ion attached to amino acid residue- for example: ceruloplamin, which contains copper

47

mucoprotein

proteins linked with large, complex carbohydrates (>4% of total weight)

48

multiple myeloma

cancer of plasma cells in bone marrow

49

nucleoprotein

combination of simple protein and nucleic acids (DNA, RNA)

50

ochronosis

darkening of skin, urine, and connective tissues of body because of excess homogentisic acid in patients with alkaptonuria

51

peptide

molecule containing two or more amino acids

52

peptide bond

bond that links amino acids in proteins; a molecule of water is split between the carboxyl group of one amino acid and the amino group of another, and a covalent bond is formed

53

phenylketonuria (PKU)

inborn error of metabolism, an autosomal recessive trait , that results in inability to metabolize essential amino acid phenylalanine to tyrosine; phenylalanine accumulates in body and results in severe neurological defects (mental retardation) in infant if not recognized and treated

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primary stucture

protein structure determined by sequence and specific order of amino acids in ploypeptide chain

55

protein electropheresis

movement of charged particles through medium in which they dispersed because of changes in their charges or electrical potential; proteins are negatively charged because of buffer pH (8.6) and thus migrate to anode

56

protein-energy malnutrition (PEM)

malnutrition from inadequate protein intake; people at risk for PEM are elderly, hospitalized, or nursing home patients and those with chronic illnesses (diabetes, arthritis), increased nutritional losses, open wounds, burns, and malabsorption (gastrointestinal protein-losing diseases)

57

proteinuria

increase in urinary protein resulting from renal or systemic disease

58

relative hyperproteinemia

hyperproteinemia in which protein concentration is usually normal but dissolved in less plasma

59

relative hypoproteinemia

form of hypoprotenemia that occurs in water intoxication, salt-retention syndromes, and as result of massive IV infusions and administration of volume expanders (e.g. dextran)

60

secondary structure

protein structure determined by interaction of adjacent amino acids; affected by winding of polypeptide chain, formation of hydrogen bonds between NH and CO groups of peptide bonds, and occasional disulfide bonds

61

secretory IgA

second form of IgA found in secretions, inculding tears, sweat, saliva, and milk as well as gastrointestinal and bronchial secretions

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simple protein

protein composed only of amino acids (albumin, for example)

63

spina bifida

congenital defect in walls of spine that allows protrusion of spinal cord or meninges

64

transferrin (TRF)

major component of β-globulins and principal plasma protein for transport of ferric iron (Fe³⁺) from intestine, where it is absorbed by apotransferrin to red cell precursors in bone marrow or to liver, bone marrow, or spleen for storage

65

tertiary structure

protein structure described by the way in which protein chain folds back on itself to form three-dimensional structure

66

transthyretin (TTR)

prealbumin protein that binds with thyroxine and triiodothyronine (thyroid hormones) and retinol (vitamin A) and serves as transport protein

67

wilson's disease (WD)

rare autosomal recessive trait in which ceruloplasmin levels are reduced and dialyzable copper concentration is increased; involves mutation in copper-transporting ATPase (ATP7B) that moves copper into bile for excretion; copper accumulates in various organs (e.g., brain, liver, kidney, and cornea); associated with degenerative changes in the brain, cirrhosis, splenomegaly, involuntary movements, psychic disturbances, and progressive weakness and emaciation