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includes amino group, carboxyl group, hydrogen and R group

1. patient presents
2. total serum
3. albumin level (albumin/globulin levels)
4. if a/g abnormal then do serum protein electrophoresis
5. if Serum pe is normal then do urine PE
if Urine PE is normal there is no problem

Norm is greater than one. anything less than one is indicator of disease.

If liver malfunctions Alb goes down, but total unaffected.

Hyperproteinemia-lots of protein in blood stream
causes: dehydration (proportionate decrease in all fractions
or multiple myeloma-increases in one clone of Ig but alb does not change->low alb/glu

Hypoproteinemia-
decrease protein in blood
alb/glb ratio decreased

decreased intake-malnutrition or malabsorption-=-> no change or decrease in ratio

Norm is greater than one. anything less than one is indicator of disease.

If liver malfunctions Alb goes down, but total unaffected.

Hyperproteinemia-lots of protein in blood stream
causes: dehydration (proportionate decrease in all fractions
or multiple myeloma-increases in one clone of Ig but alb does not change->low alb/glu

Hypoproteinemia-
decrease protein in blood
alb/glb ratio decreased

decreased intake-malnutrition or malabsorption-=-> no change or decrease in ratio

uses bacillus subtilis and beta 2 thienylalamine on a medium.

betal 2 theinylalmine

The bacteria grows on the plate.

because the extra phenylalanine created in infants with PKU inhibits the b-2 thienylanamine which inhibits growth (double negative=postive growth)

inhibits fumurate synthesis pathway

fumarylacetoacetate hydrolase defficiency which produces the byproducts succinyl acetoacetate, and succinyl acetone

symptoms includ cabbage like odor ricketts, failure to thrive

inhibits fumarate synthesis pathway

caused by homogentisate oxidase deficieny

causes buildup of homogentisic acid

symptoms include benign igment deposit->arthritis
andnd brown/black urine

changes in diet for treatment (low in tyrosine/phenylalanine)

block in anabolisis of branched chain amino acids

can't changed branced alpha keto acids to CoA deriviatives because of lack in alpha ketoacid dehydrogenase deficiency

branched chain ketoacids create maple syrup (ketones smell sweet)

symptoms-difficult to feed, vomiting, lethargy, ketosis, urin smells like maple syrup, neuro damage,

treatment-diet of mixed pure amino acids

block in methionine to cystein chain

type I homocystinuria can't change homocystein to cystathionine because of lack of cystathione synthase.

homocysteine builds up and is excreted in urine

symptoms-thrombosis, osteoporosis, dislocated lens, mental retardation, scoliosis, concave in chest

treatment-diet- restricted methionine, increased cystein, high vitamin B6

The carboxyl of one aa and the amino group of another condense (lose h20) an dform peptide bond. so chain is NCC NCC. peptide bond is shorter and stronger than the CN bond.

the CCNC bonds are in a plane

primary-chain of amino acids, not functional, but eventually determines structure

secondary- alpha helix or beta pleated sheets, formed by h bonding with itself (alpha) or between chains (beta)

Tertiary- folding of a chain and secondary structure to form subunits, uses disulfide bonds, hphobic/hphilic interactions

quarternary-very functional form of protein-spacial arrangement of subunits via diverse bonding mechanisms

reference method that finds nitrogen in a sample to find amount of protein

sometimes a problem bc n is sometimes in r group

protein and sulfuric acid heated and added to acid until ammonia forms. measure ammonia to find nitrogen content

in 8.6 solution, acids are negative and go to positive pole(cathode).

The largest/closest to (+) is albumin, followed by alpha 1, alpha2 bumps of about a quarter of the size followed by beta, a little smaller and a wide spread gamma charge.

albumin, alpha 1, alpha 2, beta, gamma

maintains colloidal osmotic pressure and is a transport protein

is a negative acute phase protein meaning if bump is smaller there's probably some sort of inflammation. when it is decrease there is less osmotic pressure and edema increases

includes alpha1 antitrypsin which inhibits trypsin, if low it indicates emphysema, but if high it indicates inflammation (acute phase protein

alpha 1 acid glycoprotein increases in cronic inflamation and increases a lot in malignant disease (acute phase protein

alpha 1 fetoprotein-fetal protein at embryonic stage, increases in maternal serum and amniotic fluid lead to fetal open neural tube defect, extreme rises in adults indicates hepatocellular or germ cell carcinoma. if decreased in embryo, may cause down's syndrome

increases

alpha macroglobulin- inhibits trypsin which lead to dephrotic syndrome which leads to loss of protein. also increases in cirrhosis and diabete millitus

haptoglobin- binds to free hemoglobin and is lowered in hemolytic anemia, but increased in inflammation (acute phase protein)

ceruloplasmin binds copper and is lwoered in disease and increase in inflammation (acute phase protein)

transferrin-binds and transports iron, raised in iron defiiciney anemia, lowers in acute phase reaction

complement- acute phase protein, lowers in auto immune disease

immuno globulins
C reactive protein-increase in inflammation

alpha 1 antitrypsin -2
alpha 1 acid glycoprotein
haptoglobin
ceruloplasmin
complement-3 (C3 especially)
fibrinogen
CRP-biggest and most responsive

protein like substances like Ig's or Ig light chains. presence indicates multiple myeloma

one very large spike in EP that is not albumin that indicates monoclonal expansion

infections, autoimmune diseases, or neoplasms

multiple myelomas- (decreased normal plasma cells) decreased antibodiesholes in bones lead to calcium release) and . elevated monoclonal Ig's in serum/urine. must have 1 major and 1 minor indicator or 3 minor indicators
waldenstrom's macroglobulinemia (IgM class malignancy) causes fatigue mucous membrane bleeding and enlarged lymph nodes and spleen-increased protein/viscosity, normochromic/normocytic anemia, rouleaux blood smear, hypercellular bone marrow, lots of IgM (plasmaphoresis and chemo)

clone of differentiated B cells creates Ig with either light chain only or heavy chain only

all proteins lowered but alpha 2 (high haptoglobin and high alpha 2 amcroglobulin)

little lower albumin
increase in alpha1 and alpha 2
beta may change (transferrin lowers but c3/c4 raise)
gamma increase (increased crp)

creases beta gamma bridge and lowers albumin because it's made in liver. (IgA, M and G increased)

lowered albumin, but one huge M spike.

lots of albumin (glomerular filtration) with a little uromucoid (tubular secretion) and minor other proteins

50-80 gm/day (at rest)

15-45 mg/dL

low moleular weight plasma proteins

retinal binding protein, albumin transferrin, IgG and other come from outside of the cavity

transferrin, IgG are synthesized intrathecally.

possible multiple myeloma

Calcium produced by holes in bones, Red blood cells are decreased

has decreased plasma cells so reoccuring infection is caused by no Ab's, platelets are low because of thromboocytothemia

many kinds of clones being produced Antigen causes multiple types of Ab's to be created. Ab's target one epitope so many Ab's react to same Ag

caused by infection autoimmune disease or neoplasm

albumin
transferrin

method for finding amount of protein in sample

add copper and biuret. copper crosslinks C=O groups.

must have a tripeptide to be detected because in order to crosslink the c=o's there has to be that many.

test shows c=o's not just amino acids

principe: light changes direction when passing from one medium to another. more protein more refraction sin theta incidence/sin theta r

sources of error-altered proteins, hemolysis, temperature (as temp increases RI decreases, standard and sample should be same temp,

Sensitivity: high concentrations (grams/dL)

principle: reduction of light transmitted (light blocked)
protein must be exposed to weak acid to create particulate proteins suspended

sources error: # and cross sectional area of particles, timing (longer you let sit, the more transmittance), temp- high temp makes particulates faster and more likely to deflect light, problems with alb/ glob ratio

sensitivity low concentrations (mg/dL) good for urine and spinal fluid

1. transport of amino acids across cell membrantes to be assembled
2. synthesis of glutathione (which is glutamyl reduced by NADPH)

antioxidant, iron in ferrous state, cell membrane structure

hemolytic anemias because of lack of cell membrane support.

inborn errors of amino acid metabolism

includes: PKU, thyrosinemia, alkaptonuria, maple syrup urine diseases and homocystinuria

-Type 1-Phenylalanine hydroxylase deficiency
-Type 4 and 5- dihydropteridine reductase deficiency

changing tyrosine to phenylalanine

mental retardation, impaired psychomotor development, light/fair skina and blue eyes (bc phenylalanine makes melanin, no melanin, no tint), musty odor (increased phenylacetate) seizures, hyperactivity

Guthrie Test, Tandem Mass Spec and others (ELISA, chromatograph, fluorometric)

Guthrie Test, Tandem Mass Spec and others (ELISA, chromatograph, fluorometric)

Guthrie Test, Tandem Mass Spec and others (ELISA, chromatograph, fluorometric)

Guthrie Test, Tandem Mass Spec and others (ELISA, chromatograph, fluorometric)

aka ampholyte

a molecule that can be turned into a negative or poisitive ion (amino acids are zwitterions)

in acids a.a. becomes positive and in bases amino acid becomes negative

isoelectric point

pH at which molecule has no charge

kinks in amino acid chains

glyceine, alanine, proline, valine, methionine, isoleucine, leucine, tryptophan

tryptophan, phenyalanine, cysteine, threonine, serine, gutamine, asparagine

aspartic acids, glutamic acids

lysine, arginine, sometimes histidine (depends on pH)

go to surface of molecule-->wants to be closest to water

1. Biosynthesis-proteins and other (heme, nucleotides, amino acids, hormones)
2. Energy-Keto and Glucogenic

Keto -enters at acetyl Co A with Acetoacetyl CoA (fat pathway)

Glucogenic-enters as pyruvate

both types of energy contribute to kreb's cycle and create NH2 as a waste product which is disposed of in urea

pepsinogen + acid > pepsin

pepsin + protein> peptides and a few free amino acids

trypsinogen (inactive) + enterokinase (from intestines)> trypsin (active)

Trypsin + Pancreatic zymogens (inactive)>proteases