Term
| what is the job of a catalyst |
|
Definition
| increse the rate of a reaction without being changed itself |
|
|
Term
|
Definition
| reactions would be too slow |
|
|
Term
|
Definition
| usually protine, sometimes ribozymes |
|
|
Term
| what is the reactant called in an enzyme reaction |
|
Definition
|
|
Term
| what are some of the common ways to name enzymes |
|
Definition
| "substrate"-ase, "substrate + reaction description"-ase, "random other common name" |
|
|
Term
| describe the systemic way to name enzymes |
|
Definition
| "systemic name"-ase, "substrate: substrate systemic category"-ase |
|
|
Term
| what does a one way arrow in an enzyme reaction indicate |
|
Definition
| under normal human conditions the reaction goes in that direction, it could go the other way in reality but it isnt likley |
|
|
Term
| what does a double sided arrow in an enzyme reaction indicate |
|
Definition
| under normal human conditions, the reaction can go in either direction |
|
|
Term
|
Definition
| pocket of an enzyme that binds a substrate with amino acid compliments to it |
|
|
Term
|
Definition
| enzyme substrate complex: enzyme bound to substrate in a new conformation to facilitate catalysis |
|
|
Term
|
Definition
| enzyme product: dissociates into enzyme and product |
|
|
Term
| what is a way we can measure the catalytic efficiency |
|
Definition
|
|
Term
| what is the turn over number |
|
Definition
| number of molecules of substrate converted to product per enzyme per second |
|
|
Term
| what is the abreviation for turn over number |
|
Definition
|
|
Term
| how do enzymes display specificity |
|
Definition
| they only allow one or few substrates (similar structure), only do one type of reaction |
|
|
Term
|
Definition
| enzyme and its non-protein component |
|
|
Term
| what is an name for an active enzyme |
|
Definition
|
|
Term
|
Definition
| enzyme without its non protein component |
|
|
Term
| what is a name for an inactive enyme |
|
Definition
|
|
Term
|
Definition
| non-protein component of an enzyme made of metal |
|
|
Term
|
Definition
| non-protein component of an enzyme made of organic molecules |
|
|
Term
|
Definition
|
|
Term
| what are some examples of coenzymes |
|
Definition
| niacin makes NAD+, riboflavin makes FAD |
|
|
Term
| what is the point of the non-protein component of an enzyme |
|
Definition
| some enzymes need these (cofactor, coenzyme) to work |
|
|
Term
| how are enzymes regulated |
|
Definition
| activated or inhibited based on cell need |
|
|
Term
| what is the energy barrier |
|
Definition
| energy difference between that of reactants and a high energy intermediate that occurs during the formation of the product |
|
|
Term
| what does a high free energy of activation mean |
|
Definition
|
|
Term
| what do enzymes do to the free energy of activation |
|
Definition
| lower it, NOT change it. it accelerates the rate of the reaction but does not change the equlibruim |
|
|
Term
| desctibe the location of enzymes |
|
Definition
| specific subcellular compartments near organells, isolating substrates and products from competing reactions, organizes them into purposeful pathways |
|
|
Term
| what does it mean when we say that an enzyme "stabilizes the transition state" |
|
Definition
| holds substrate in conformation of high energy between substrate and product, increasing the concentration of the transition state and making it more likley that it will turn into product but giving chemical groups that participate in reaction to substrate and facilitate the form of the transition state |
|
|
Term
| what is the enzyme velocity |
|
Definition
| number of substrate that turns to product per unit time |
|
|
Term
| what is the normal units for enzyme velocity |
|
Definition
| micro mol / product / min |
|
|
Term
| what is maximal enzyme velocity |
|
Definition
| rate of enzyme catalization of a reaction with increasing substrate concentration until it reaches a max, all binding sites full, enzyme is saturated |
|
|
Term
| what is the hyperbolic curve |
|
Definition
| curve most enzymes follow. |
|
|
Term
| what are the axies of the hyperbolic curve |
|
Definition
| initial velocity (Vo) vs concentration of substrate |
|
|
Term
| what is the name of the principal that outlines the governing of the hyperbolic curve |
|
Definition
|
|
Term
| what does increasing the temperature around an enzyme do |
|
Definition
| increases velocity until a peak then decreases it making the molecules more high energy to breach activation energy until the peak which denatures |
|
|
Term
| what happens when an enzyme is denatured |
|
Definition
|
|
Term
| what is the normal temperature good for human enzymes |
|
Definition
|
|
Term
| how does pH affect enzymes |
|
Definition
| enzyme substrate needs certian groups protonated or unprotonated to form a catalytic enivornment, changes in pH can change protonation and ionic interactions denaturing the enzyme |
|
|
Term
| what is the optimum pH for an enzyme |
|
Definition
|
|
Term
| what is the reaction model in michaels menten reactions (word explination) |
|
Definition
| enzyme reversably combines with substrate to make complex that yields product and the free enzyme |
|
|
Term
| what is the reaction model in michaels menten reactions (reaction explination) |
|
Definition
|
|
Term
|
Definition
| the rate constant of the forward reaction in a michaels menten reaction when enzyme combines with substrate |
|
|
Term
|
Definition
| the rate constant of the reverse reaction in a michaels menten reaction when enzyme dissociates from substrate |
|
|
Term
|
Definition
| the forward only reaction where enzyme and substrate complex make enzyme and product in a mimchaels menten reaction |
|
|
Term
| in general, what does the michaels menten equation describe for us |
|
Definition
| how reaction velocity varies with substrate concentration at a given enzyme concentration |
|
|
Term
| what do we need to assume to make the michaels menten reaction work |
|
Definition
| amount of substrate bound by the enzyme at a given time is a small percentage of the total substrate aviable to drive the reaction forward and initial veolcity is used so there is no appreciable back reaction from product to substrate |
|
|
Term
|
Definition
| characteristic of an enzyme and particular substrate that relfects affinity of an enzyme for that substrate |
|
|
Term
|
Definition
|
|
Term
| what does a small km indicate |
|
Definition
| high affinity, so it takes a low concentration of substrate to reach 1/2 max velocity |
|
|
Term
| what does a big km indicate |
|
Definition
| low affinity, it takes lots of substrate to reach 1/2 max velocity |
|
|
Term
| how are max velocity and enzyme concentration related |
|
Definition
| they are directly proportional |
|
|
Term
| if we double enzyme concentration, what happens to max velocity |
|
Definition
|
|
Term
| if we half enzyme concentration, what happens to max velocity |
|
Definition
|
|
Term
| what does first order mean |
|
Definition
| when [S] < km, velocity is proportional to the substrate concentration and first order describes the rate |
|
|
Term
| what does zero order mean |
|
Definition
| when [S] > km, velocity is approx constant and equal to max velocity and independent of [S] making it zero order in respect to the substrate |
|
|
Term
| what is a lineweaver burk plot |
|
Definition
| inverse of michaelis menten |
|
|
Term
| what are the axis of a lineweaver burk plot |
|
Definition
|
|
Term
| what is the shape of a lineweaver burk plot |
|
Definition
|
|
Term
| what can we directly determinie from a lineweaver burk plot |
|
Definition
|
|
Term
| why do we need the lineweaver burk plot |
|
Definition
| because of the parabolic nature of the michaiels menten plot, Vmax is difficult to percisley determine |
|
|
Term
| what is the X axis on a lineweaver burk plot |
|
Definition
|
|
Term
| what is the y axis on a lineweaver burk plot |
|
Definition
|
|
Term
| in addition of Km and Vmax, what is a lineweaver burk plot useful for |
|
Definition
| determining mechanisms of action of enzyme inhibitors |
|
|
Term
| what happens in Km or Vmax increases to a linweaver burk plot |
|
Definition
|
|
Term
| what happens in Km or Vmax decreases to a linweaver burk plot |
|
Definition
| they will get further from 0 |
|
|
Term
|
Definition
| any substance that can diminish the velocity of an enzyme catalyzed reaction |
|
|
Term
| what does an irreversible inhibitor do |
|
Definition
| binds to enzymes through covalent bonds irreversibly |
|
|
Term
| what does a reversible inhibitor do |
|
Definition
| usually binds with non-covalent bonds and possibly covalent as long as the enzyme can be recovered |
|
|
Term
| what are the two types of reversible inhibitors |
|
Definition
| competitive and noncompetitive |
|
|
Term
| what does a competitive inhibitor do |
|
Definition
| binds reversibly to the same site that the substrate would normally occupy |
|
|
Term
| how does a competitive inhibitor affect Vmax, why |
|
Definition
| the effect of a competitive inhibitor can be overcome with lots of substrate so it does not affect Vmax because we assume there is unlimited substrate |
|
|
Term
| how does a competitive inhibitor affect Km, why |
|
Definition
| it increases the Km because most substrate is needed to achieve 1/2Vmax so the apparent affinity is lower |
|
|
Term
| on the graph for competitive inhibitors, what happens to the 1/Vmax point |
|
Definition
|
|
Term
| on the graph for competitive inhibitors, what happens to the -1/Km point |
|
Definition
| it becomes more negative (closer to zero) |
|
|
Term
| what is an example of a competitive inhibitor |
|
Definition
|
|
Term
| explain how statin drugs do competitive inhibition, what is the biological significance |
|
Definition
| statin is a structural analog to HMG CoA reductase which is involved in cholesterol synthesis so it competes for its active site, lowering cholesterol |
|
|
Term
| how does a noncompetitive inhibitor work |
|
Definition
| inhibitor binds reversibly to a site other than the substrate binding site, it can bind wether the substrate is bound or not |
|
|
Term
| how do noncompetitive inhibitors affect Vmax, why |
|
Definition
| they cannot be overcome by increasing substrate so they lower the Vmax |
|
|
Term
| how do noncompetitive inhibitors affect Km |
|
Definition
| they do not interfere with the binding of the substrate so it does not change the affinity, no affect |
|
|
Term
| what happens to the point -1/km on the graph due to a noncompetitive inhibitor |
|
Definition
|
|
Term
| what happens to the point 1/Vmax on the graph due to a noncompetitive inhibitor |
|
Definition
| it increases in Y value, it gets further from zero |
|
|
Term
| what is an example of a noncompetitive inhibitor |
|
Definition
|
|
Term
| explain how ferrochelatase does noncompetitive inhibition |
|
Definition
| it inserts Fe into the protophoryin which makes heme, fe noncompetitivly inhibits ferrocheletase by binding its sulfhydril groups on cystine stopping Fe getting into heme |
|
|
Term
| why is the rate of enzymes in the body affected by the concentration of the substrate |
|
Definition
| because physiological substrate is near the range of Km so an increase will prompt proportional increase in rate and vice verse. |
|
|
Term
| how a allosteric enzymes regulated |
|
Definition
|
|
Term
|
Definition
| they bind to sites other than the active site on enzymes altering their affinity to substrate (affect Km) or the catalytic activity (Vmax) or both |
|
|
Term
| what is a negative effector do |
|
Definition
| inhibit allosteric enzyme activity, decrease Vmax or increase Km |
|
|
Term
| what does a positive effector do |
|
Definition
| increase allosteric enzyme activity, increase Vmax or decrease km |
|
|
Term
| what is a homotrophic effector |
|
Definition
| when the substrate itself serves as an effector, most often positivly. alters the other binding sites of the enzyme changing their Km or Vmax |
|
|
Term
| what is another name for homotrophic effectrs actions |
|
Definition
|
|
Term
| what type of curve demonstrates cooperitivity |
|
Definition
|
|
Term
| what is an example of coopertivity |
|
Definition
|
|
Term
| what is a heterotrphic effector |
|
Definition
| effector is different than the substrate, possibly a product inhibiting the rate limiting step, binding the enzyme at a site other than the active site |
|
|
Term
| what is an example of a heterotrphic effector |
|
Definition
| PFK-1 is the rate limiting step in glycolysis, citrate from the TCA cycle can shut this step down if it builds up making the sythesis of glycogen vs glucose |
|
|
Term
| what is the most common form of enzyme regulation |
|
Definition
| covalent modification usually via phosphorlyation or dephosphorlyzation of the SER, ThR, or TYR -OH group |
|
|
Term
|
Definition
|
|
Term
| what does a phosphatase do |
|
Definition
|
|
Term
| what does fasting cause in metabolic enzymes |
|
Definition
| activates phosphorlyating kinases, activates catabolism and inhibiting anabolism |
|
|
Term
| what does a well fed state do to metabolic enzymes |
|
Definition
| inhibits phosphorylzation, deophsphorlyzation activated. activates anabolism and inhibiting catabolism |
|
|
Term
| explain how induction or repression can control enzymes |
|
Definition
| you can alter their synthesis by controling their gene expression or their degredation by controling other genes |
|
|
Term
| what qualifies an enzyme to be regulated by induction or repression of expression |
|
Definition
| it usually needs to be under specific physiological conditions and not in constant use |
|
|
Term
| how long does it take for gene alteration to control enzymes |
|
Definition
|
|
Term
| how long does it take for covalent measures to change enzyme activity |
|
Definition
|
|
Term
| why are steroids not immediatly effective |
|
Definition
| because they control gene expression not covalent modifications to enzymes |
|
|
Term
| describe the normal enzyme component of the blood |
|
Definition
| there are a small amount for things like coagulation and a teeny bit because of cell lysis and turn over |
|
|
Term
| why is having some enzymes from cell lysis and turn over in the blood ok |
|
Definition
| because they are normally removed |
|
|
Term
| when is having some enzymes from cell lysis and turn over in the blood a problem, what does this cause, what is it caused by |
|
Definition
| when they are not removed and build up, tissue damage, disease |
|
|
Term
| how can you determine the extent of tissue damage using plasma and where it came from |
|
Definition
| count the levels of enzymes from lysed cells, cells have specific enzymes so can you look at the type to see where they lysed from |
|
|
Term
|
Definition
| caralyze the same reaction but are a different on the amino acid level, they may also have different quatrentary subunits |
|
|
Term
| how can you find isoenzymes vs enzymes in the lab |
|
Definition
| electrophoreses, different amino acids give different weights |
|
|
Term
| why are isoenzymes useful |
|
Definition
| different organs have specific ones and can indicate the location of disease |
|
|
Term
| What type of effector is a homotroohic effector |
|
Definition
|
|
Term
| How does a homotroohic effector work |
|
Definition
| Substrate itself is the effector |
|
|
Term
| What does a homotroohic effector do to Vmax and Km |
|
Definition
| Increases Vmax and decreases Km of other substrate binding sites |
|
|
Term
| What is the shape of a curve for homotroohic effectors |
|
Definition
| Sigmoidal when Vo vs substrate concentration |
|
|
Term
| What type of effector shows cooperatively |
|
Definition
|
|
Term
| How does a heterotrophic effector work |
|
Definition
| Effector is different than the substrate |
|
|
Term
| Is a heterotrophic effector positive or negative |
|
Definition
|
|
Term
| What does heterotrophic effectors show is going on in the reaction |
|
Definition
|
|
Term
| What is feedback inhibition |
|
Definition
| Accumulation of product inhibits rate limiting step at a location other than a binding site for the substrate |
|
|
Term
| What is an example of feedback inhibition |
|
Definition
| PFK-1 is rate limiting step in glycolysis, citrate from the CAC can inhibit this step changing from production of glucose to glycogen |
|
|
Term
| How is covalent modification of enzymes done |
|
Definition
| Phosphorlyation or desphosphorlyation of -OH of ser, the, and tyr |
|
|
Term
|
Definition
|
|
Term
|
Definition
|
|
Term
| Does phosphorylation turn on or off genes |
|
Definition
| Either depending on the situation |
|
|
Term
| When fasting what enzyme is being inhibited, what enzyme is activated |
|
Definition
| Anabolic pathways were inhibited, kinases activated |
|
|
Term
| When well fed what pathway is inhibited, what enzyme is activated |
|
Definition
| Catabolism is inhibited, desphosphorlyation enzymes are activated |
|
|
Term
| What are ways other than phosphorylation we can regulate enzymes |
|
Definition
| Control transcription, control mRNA, altering gene expression (control synthesis or degration), |
|
|
Term
| What limits when we. An alter gene expression to control enzymes |
|
Definition
| You cannot do it for enzymes that are used all the time to make energy |
|
|
Term
| Way is the difference between the timing of covalent and genetic alterations to enzymes |
|
Definition
| Covalent takes minutes, genetics take hours |
|
|
Term
| What are the reasons enzymes are in the blood |
|
Definition
| Fragments due to cell lysis, normal blood enzymes like for clotting |
|
|
Term
| Why are the enzymes due to cell lysis in the blood medically significant |
|
Definition
| Normally the enzymes are removed so an increase in level can indicate tissue damage in the tissue that enzyme correlates to |
|
|
Term
|
Definition
| Enzyme that catalyzes the same reaction but uses different amino acids to do it and may have a different quaternary structure |
|
|
Term
| How can you identify isoenzymes from other enzymes |
|
Definition
| If you do electrophoresis they will be a different weight due to their difference in size t the enzyme they are like |
|
|
Term
|
Definition
| A prosthetic group tightly bound to a protein |
|
|
Term
| What is a prosthetic group |
|
Definition
| Coenzyme permeability associated with the enzyme or another protein and is returned to original form |
|
|
Term
| What does heme do in cytochromes |
|
Definition
| Electron carrier function, lots in ETC |
|
|
Term
| What does heme do in catalyase |
|
Definition
| Proximal enzyme. Breaks down hydrogen peroxide to water and oxygen |
|
|
Term
| What is the shape of a heme called |
|
Definition
|
|
Term
| What a thte bonds in the iron of heme bound to |
|
Definition
| 4 nitrogens bind to iron, 1 to hb or myoglobin on r group of HIs of globin, binds oxygen |
|
|
Term
| Where is myoglobin found in the body |
|
Definition
| Cardiac and skeletal muscle |
|
|
Term
| What is the function of myoglobin |
|
Definition
| Binds oxygen very tight, only releases oxygen if the body is very low in it, it's high affinity can change the rate of diffusion in the cell |
|
|
Term
| Describe the structure of myoglobin |
|
Definition
| One chain similar to aha or beta, interior non polar site with his that binds 1 oxygen and a his that binds iron of heme, polar amino acids on surface |
|
|
Term
|
Definition
|
|
Term
| how many oxygen does a hemoglobin transport |
|
Definition
|
|
Term
| how many oxygen does a myoglobin transport |
|
Definition
|
|
Term
| what kinds of molecules can a hemoglobin transport |
|
Definition
| oxygen, CO2, H+, 23-BPG, bicarbonate |
|
|
Term
| what mechanism regulates the oxygen binding site on heme |
|
Definition
|
|
Term
| describe the quaternary structure of hemoglobin |
|
Definition
|
|
Term
| what is the state of the hemoglobin in the T form |
|
Definition
| deoxygenated, lower oxygen affinity, rigid |
|
|
Term
| dscribe the bonds of a hemoglobin in the T form |
|
Definition
| strong hydrophobic bonds between the alpha and beta chains. weak ionic and hydrogen bonds between the two alpga beta dimers |
|
|
Term
| what is the state of hemoglobin in the R form |
|
Definition
| oxygenated, high oxygen affinity, relaxed |
|
|
Term
| describe the bonds of a hemoglobin in the R form |
|
Definition
| the bonds within the dimers will be the same but the ionic and hydrogen ones between the dimers will lessen |
|
|
Term
| when looking at a hemoglobin curve, what location in the body does the left side indicate |
|
Definition
|
|
Term
| when looking at a hemoglobin curve, what location in the body does the right side indicate |
|
Definition
|
|
Term
| what is the shape of a hemoglobin curve |
|
Definition
|
|
Term
| what is the shape of a myoglobin curve |
|
Definition
|
|
Term
| what are the axis on a hemoglobin coopertivity graph |
|
Definition
| partial pressure of o2 (mmHg) vs degree of saturation of O2 |
|
|
Term
|
Definition
| partial pressure of oxygen to achieve half the saturation in the atmosphere |
|
|
Term
| what does a low P50 indicate |
|
Definition
|
|
Term
| what does a high P50 indicate |
|
Definition
|
|
Term
| in general, what does it mean if a Hb curve is shifted left |
|
Definition
| binds oxygen with higher affinity |
|
|
Term
| in general, what does it mean if a Hb curve is shifted right |
|
Definition
| more oxygen is released, less is bound to Hb. less degree of saturation in the lungs |
|
|
Term
| what shift of a Hb curve is generally more benificial |
|
Definition
|
|
Term
| myoglibin P50 is usually _____. why? |
|
Definition
| low, because of the higher affinity it has for oxygen |
|
|
Term
| what are two important examples of cooperative biniding |
|
Definition
| hemoglobin and allosteric enzymes |
|
|
Term
| what is the heme-heme interaction |
|
Definition
| interaction on one site of Hb makes other sites increase their affinity for Hb allowing more oxygen to be delivered to the tissues in response to small changes in pO2 |
|
|
Term
| what does the pO2 in the tissues allow |
|
Definition
|
|
Term
| what does the pO2 in the lungs allow |
|
Definition
|
|
Term
|
Definition
| Hb has less affinity for oxygen at lower pH values shifting the curve right, unloading more oxygen. a greater pO2 is needed to achieve the same oxygen saturation |
|
|
Term
| what can cause lower blood pH and this the bohr effect |
|
Definition
|
|
Term
| what activity of Hb is favored at a low pH |
|
Definition
|
|
Term
| what activity of Hb is favored at high pH |
|
Definition
|
|
Term
| what is the bicarbonate reaction |
|
Definition
| CO2 + H2O -> H2CO3 -> HCO3 + H+ |
|
|
Term
| why does the Hb assume the T state without oxygen |
|
Definition
| because the pKa of his shifts without O2 so it cannot bind proteins as well, this stabilizes the T state leading to less oxygen affinity |
|
|
Term
| when in the T state, which way is the curve shifted |
|
Definition
|
|
Term
| how and where is 2,3-BPG made |
|
Definition
| product of glycolysis in RBC |
|
|
Term
| what does 2,3-BPG bind do |
|
Definition
|
|
Term
| what function does 2,3-BPG play |
|
Definition
| stabilizes the T form of Hb, decreasing oxygen affinity |
|
|
Term
|
Definition
| at picket between B globin chains to positive amino acids because they are negative |
|
|
Term
| what happens to 2,3-BPG when oxygen binds a Hb |
|
Definition
| it is expelled from the Hb |
|
|
Term
| what does 2,3-BPG do to the Hb curve |
|
Definition
|
|
Term
| what action does 2,3-Bpg help the Hb do |
|
Definition
| unload oxygen into tissues |
|
|
Term
| what diseases can cause the body to make more 2,3-BPG |
|
Definition
| chronic hypoxia, COPD, emphysima, high altitudes, anemia, hypoxia |
|
|
Term
| what do lung function decreasing diseases do to 2,3-BPG and the Hb curve |
|
Definition
| cause the body to make more of it, shifting it right |
|
|
Term
| when someone gets a blood transfusion, why for ~6 hours do they have problems letting their O2 go into the tissues |
|
Definition
| the transfused blood had the 2,3-BPG mostly deteroirate, after about 6 hours it builds back up. initially, the transfused blood will not release oxygen well |
|
|
Term
| what does the curve look like when someone has just had a blood transfusion, does it shift? |
|
Definition
| it is more like myoglobin, it is only slightly sigmoidal, shifts left |
|
|
Term
|
Definition
| it travels in the form of bicarbonate and when attached is a carbamate on the N terminal of AA of Hb turning the Hb into carbaminohemoglobin |
|
|
Term
| what is the equation for CO2 Hb interaction |
|
Definition
| Hb-NH2 + CO2 -> Hb-NH-COO` + H+ |
|
|
Term
| what effect does CO2 have on the structure of Hb |
|
Definition
|
|
Term
| what does CO2 do to the Hb curve |
|
Definition
|
|
Term
| what does CO2 do to the Hb affinity |
|
Definition
|
|
Term
| what does Hb have a higher affinity for: O2, CO2, 2,3-BPG, or CO |
|
Definition
|
|
Term
|
Definition
| at the oxygen binding site |
|
|
Term
| when CO attaches to Hb what physical changes does it cause |
|
Definition
| Hb goes into the R state, now has a higher affinity for oxygen or CO, whatever, less unloading |
|
|
Term
| what does CO do to the Hb curve |
|
Definition
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|
Term
| describe the structure of fetal Hb, what does this cause |
|
Definition
| gamma chains lack some of the AA that interact with 2,3-BPG so low affinity for it provides a higher oxygen affinity allowing baby to steal O2 from mom |
|
|
Term
| what is the function of HbA2 |
|
Definition
|
|
Term
| what is another name for HbA1c |
|
Definition
| modified adult hemoglobin |
|
|
Term
|
Definition
| over time, adult Hb is glycosylated non enzymatically to an extent in proportion to the sugar around the RBC in their 120d |
|
|
Term
|
Definition
| it someone has been following their diabetes diet or it it isnt working |
|
|
Term
| what percent of Hb is FHb, HbA2, and HbA1c in an adult |
|
Definition
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|
Term
| what is the most common inherited blood disorder |
|
Definition
|
|
Term
| when do the symptoms for sickle cell appear, why |
|
Definition
| around 6 mo old because the issue is with beta globin and you dont replace gamme globin with beta until then |
|
|
Term
| what are the symptoms of sickle cell |
|
Definition
| apisodes or crises (pain), chronic hemolytic anemia, increased susceptability to infection |
|
|
Term
| how long does a sickle cell live |
|
Definition
|
|
Term
| what is the exact mutation inoved in sickel cell, mutated to what |
|
Definition
| glutamate is replaced with valing going from negative to neutral |
|
|
Term
| how can you seperate sickle cell Hb and normal |
|
Definition
| electrophoresis because they are different weights |
|
|
Term
| what does the chance in amino acid in sickle cell cause structurarly |
|
Definition
| makes a pocket in b globin so it can bind to another Hb making Hb fibrils causing the cell to sickle only when the cell is deoxygenated |
|
|
Term
| why do sickled cells cause problems |
|
Definition
| they dont flow normally and stick to eachother and the walls, they cannot pass through small capilaries due to their rigidity |
|
|
Term
|
Definition
| pain from trying to smoosh sickle cells through capillaries |
|
|
Term
| what can increase severity of sickling in sickle cell anemia |
|
Definition
| anything that puts Hb in the deoxy state: high altitudes, flying in a non-pressurized plane, increasing CO2, decreasing pH, increasing 2,3-BPG |
|
|
Term
| what does dehydration do to someone with sickle cell |
|
Definition
| decreases blood flow causing less movement of oxygen and more Hb unloading, more Hb will be in deoxy form increasing sickling |
|
|
Term
| what can exercise to do someone with sickle cell |
|
Definition
| decreases pH / CO2 and causes more sickling |
|
|
Term
| what are some treatments for sickle cell |
|
Definition
| hydration, analgesic, antibiotic therapy, blood transfusion, hydroxyurea |
|
|
Term
|
Definition
|
|
Term
| what mutation happens in Hb C disease |
|
Definition
| lysine is substituted for glutamate (in the same spot as sickle cell) |
|
|
Term
| what are the symptoms of homozygous HbC disease |
|
Definition
| mild chronic hemolytic anemia, no infractive crises, no specific therapy |
|
|
Term
| what mutation happens in Hb SC disease |
|
Definition
| patient inherits one copy of HbS and one of HBC |
|
|
Term
| what are the symptoms of Hb SC disease |
|
Definition
| symptoms are more variable and between severe sickle cell and HbC disease. less frequent sickling leading to less frequent and severe crisis |
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