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96 Cards in this Set
- Front
- Back
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RISK FACTOR
SYMPTOM |
Probable or cause of a disease
sign or indicator of a disease |
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Positive risk factors 9 of them
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obesity
family history age sedentary lifestyle hypertension prediabetes smoking dyslipidemia |
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dyslipidemia
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LDL - 130 or more mg/dl
TC - triglcerirdes of 200 or more HDL - 40 or less mg/dl lipid lowering medication by endurance and activity and eating better cholesterol will increase your HDL GOOD and lower your LDL BAD |
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obesity
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BMI body mass index of 30kg/m2 or more
waist girth for men 102 cm - 40 in or more women 88 cm or 35 in or more waist/hip ratio of 0.95 men and 0.86 women need physical activity and calorie intake..endurance activity |
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Smoking
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2 times more at risk for heart disease than non smokers
Current smoker Quit within the last 6 months Enviornmental tobacco |
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Age
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45 or older in men and 55 or older in women
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Family History
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family member had MI myocardial infartion, coronoary revascularization coronary artery bypass surgery, or sudden death
first degree in 55 men or 65 in women daughter son fathermother sister brother |
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Hypertension (blood pressure)
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120/80 is the normal
120-139/80-89 is prehypertension 140-159/90-99 is stage 1 hypertension 160 or more/100 or more is stage 2 hypertension |
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Diastolic and Systolic blood pressure for resting blood pressure
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Systolic - Highest number during stysole in heart when a large volume of blood is ejection and empyting into the arteries
Diastolic- during diastole of the cardiac cylcle when lower number resting and filling 130/85 is not good |
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Sedenary lifestyle
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No physical activity or not meeting the recommended PA. 30 mintues most days of the week for at least 3 months
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prediabetes (blood glucose)
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fasting blood glucose - 100 or more mg/dl
impaired glucose tolerance - 140 or less after 2 hours but less than 200..confirmed measurements by 2 seperate occasions |
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metabolic syndrome
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cluster of metabolic diseases in one patient
central obesity (apple vs.pear) Elevated Triglycerides Elevated Blood Pressure Elevated Fasting Blood Glucose Low HDL cholesterol |
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contraindicators when the risk are higher than the potential benefits you should wait until they are all better
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Absolute - uncontrolled heart failure, angina
Relative - uncontrolled metabolic disease, severe hypertension |
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LOW RISK
MODERATE RISK HIGH RISK |
LOW- 1 sign or symptom of the risk factors
MODERATE- 2 or more of the sign or symptoms HIGH- known cardiovasculartory, pulmonary, or metabolic disease |
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Negative Risk factors
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HDL is the good cholesterol need 60 or more mg/dl
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Informed Content
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Confidential and voluntary
know the risk.benefits.and purpose of the PA have time for questions |
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PAR-Q and other things before the actual PA can take place
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7 yes or no questions
Physical Activity Readiness Questionnaire Given to see if you should see a physician before starting the PA Medical History, take blood sugar, triglyercides, cholestrol, resting blood pressure and heart rate |
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irreversible inhibition
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form of enzyme inhibition in which an inhibitor permanently impairs an enzyme, usually through biding via a covalent bond
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Lineweaver-Burk plot
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A graph in which Km and Vmax values for an enzyme are determined using the reciprocals of initial velocities and substrate concentration
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positive cooperativity
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The mechanism in which the binding of one ligand to a target molecule increases the likelihood of subsequent ligand binding
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negative cooperativitiy
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The binding of one ligand to a target molecule, decreasing the likelihood of subsequent ligand binding
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zymogen
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The inactive form of a proteolytic enzyme
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properties of enzymes
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The important properties of enzymes are: high catalytic rates, a high degree of substrate specificity, negligible formation of side products, and capacity for regulation.
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Cells regulate enzymatic reaction by the following
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1. Using genetic control – Certain key enzymes are synthesized in response to changing metabolic needs.
2. Covalent modification – Certain enzymes are regulated by the reversible interconversion between their active and inactive forms, a process involving covalent changes in structure. 3. Allosteric regulation – Binding effector molecules to pacemaker enzymes alters catalytic activity. 4. Compartmentation – Preventing wasteful “futile cycles” by physical separation of opposing biochemical processes within cells. |
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biochemical processes importance
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Three reasons why the regulations of biochemical processes are important are maintenance of an ordered state, conservation of energy, and responsiveness to environmental cues.
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negative pathway inhibition
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Negative pathway inhibition is a process by which the product of a pathway inhibits the activity of the pacemaker enzyme.
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The following are the major coenzymes and their function
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Vitamin- An organic molecule required by organism in minute quantities; some vitamins are coenzymes required for the function of cellular enzymes.
Cofactor- The nonprotein component of an enzyme (either inorganic ion or a coenzyme) required for catalysis Transition state- The unstable intermediate in catalysis in which the enzyme has altered the form of the substrate so that it now shares properties of both the substrate and the product Inhibitor- A molecule that reduces enzyme’s activity Allosteric enzyme- An enzyme whose activity is affected by the binding of effector molecules |
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reactions
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At the start of a reaction, the concentrations of the reactants and products can be known precisely. Since the equilibrium has not yet been established presumably only the forward action is taking place which is why the measurements can be made at the start of the reaction.
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enzymes
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Enzymes lower the activation energy of a reaction by lowering the free energy of the transition state. The active site of the enzyme described (uncatalyzed reaction rate from substrate x to product y is 1 year and enzyme-catalyzed rate is one millisecond) most likely contains amino acid residues that stabilize the transition state with some or all of the following: electrostatic effects and noncovalent interactions a shape that accepts the substrate yet eases strain in the transition state, and participation in the catalysis mechanism (ex. By providing an acidic, basic, or nucleophilic residue to assist in acid-base or covalent catalysis). The active site should also place the substrate and reactants in close proximity to each other and in the proper orientation.
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protease
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An enzyme that catalyzes the cleavage of peptide bonds with the addition of water
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hydroxylase
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An enzyme that catalyzes the insertion of an oxygen atom into a C-H bond in order to form a new hydroxyl group
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metabolon
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A complex of enzymes that share intermediates of a metabolic pathway so that the product of one enzyme is in close proximity to the active site of the next enzyme in the pathway
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Compartmentation within eukaryotic cells in the physical separation of enzymes by a membrance (by containing certain enzymes within an organelle), or by attachment of enzymes to membranes or cytoskeletal filaments. Compartmentation functions are the following;
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1. Prevents competing reactions from occurring simultaneously and allows them to be regulated separately (“divide and control”)
2. Reduces or removes diffusion barriers by locating enzymes and metabolites close to each other 3. Provides specialized reaction condition (low pH) that would not be possible otherwise 4. Protects other cellular components from potentially toxic reaction products (“damage control”) |
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active site
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The three-dimensional shape of the active site is vital to enzyme function and its ability to stabilize the transition state. A very specific structure of an enzyme is required to ensure that the active site has the optimum shape, electrostatic environment, flexibility (to optimize proximity and strain effects), and precise locations of amino acid side chains that actively participate in the enzyme’s catalytic mechanism. This complex precision of the active site structure is created and maintained by the intricate web of interactions between amino acid residues in the enzyme as a whole. The inefficiency of creating such a large molecule is tolerated because of the enormous advantage provided by the increase in reaction rates and enzyme efficiency that result.
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energy of reaction vs. energy of activation
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. The energy of a reaction is the difference between the energy of the reactants and product. The energy of activation is the energy difference between the reactants and the transition state.
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monosaccarhide
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A polyhydroxy aldehyde or ketone containing at least three carbon atoms
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aldose and ketose
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Aldose – A monosaccharide with an aldehyde functional group
1c. Ketose – A monosaccharide with a ketone functional group |
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hemiacetal
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– One of the family of organic molecules with the general formula RRC(OR)OH that is formed by the reaction of a molecule of alcohol with an aldehyde
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hemiketal
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One of the family of organic molecules with the general formula RRC(OR)OH that is formed by the reaction of a molecule of alcohol with a ketone
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anomer
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One of two possible diasterisomers that may form during the cyclization reaction of a hemiacetal or hemiketal
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furan
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An organic molecule with a five-sided ring containing one oxygen atom; pyranoses are named in reference to furan
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pyran
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An organic molecule with a six-sided ring containing one oxygen atom; pyranoses are named in reference to pyran
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lactone
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A cyclic ester
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reducing sugar
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- A sugar that can be oxidized by weak oxidizing agents
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epimerization
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The reversible interconversion of epimers
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acetal
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One of a family of organic compounds with the general formula RCH(OR’)2; formed from the reaction of a hemiacetal with an alcohol
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glycosidic link
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An acetal linkage formed between two monosaccharides linked through at least one anomeric carbon of the monosaccharides
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glycoside
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The acetal form of a sugar
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polysaccharide
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A linear or branched polymer of monosaccharides linked by glycosidic bonds
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cellobiose
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The disaccharide product of cellulose degradation; two molecules of glucose linked by β(1,4) glycosidic bond
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homoglycan
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High-molecular weight carbohydrate polymers that contain more than one kind of monosaccharide
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heteroglycan
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High-molecular weight carbohydrate polymer that contains more than one kind of monosaccharide
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amylose
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A type of plant starch; an unbranched polymer of D-glucose residues linked with α (1,4) glycosidic linkages
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amylopectin
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A type of plant starch; a branched polymer containing α(1,4) and α(1,6) glycosidic linkages
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glycogen
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A glucose storage molecule in vertebrates; a branched polymer containing α(1,4) and α (1,6) glycosidic linkages
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cellulose
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A polymer produced by plants that is composed of D-glucopyranose residues linked by β(1,) glycosidic bonds
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N-glycan
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asparagine-linked oligosaccharide
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epimer
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A molecule that differs from the configuration of another by one asymmetric carbon
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glycosidic linkage
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An acetal linkage formed between two monosaccharides
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reducing sugar
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A sugar that can be oxidized by weak oxidizing agents
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monosaccarhide
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A polyhydroxy aldehyde or ketone containing at least three carbon atoms
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anomer
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An isomer of cyclic sugar that differs from another in its configuration about the hemiacetal or acetal carbon
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starch and glycogen
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Starch and glycogen are both homoglycans containing glucose monomers linked by α-(1,4) glycosidic bonds with branch points connected by α-(1,6) glycosidic bonds. However, glycogen is more highly branched than starch. Cellulose is a linear polymer of glucose linked by β-(1,4) glycosidic bonds.
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Benedicts reagent
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. A reducing sugar reduces Cu(II) in Benedict’s reagent. This reduction takes places because the hemiacetal portion of a sugar can form an aldehyde functional group, which can be oxidized to a carboxylic acid.
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look at
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a. D-erythrose and D-threose are epimers
b. D-glucose and D-mannose are epimers c. D-ribose and L-ribose are enantiomers d. D-allose and D-galactose are diastereomers e. D-glyceraldehdy and dihydroyacetone are an aldose-ketose pair |
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Three sugars are produced by the epimerization of galactose:
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1. Talose- The sugar produced by the epimerization of galactose C2
2. Glucose – The sugar produced by the epimerization of C4 3. Galactose – The sugar produced by the epimerization of C3 |
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Moisture loss
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Moisture loss in candy is prevented because of the hydrogen bonding between the OH groups of sorbitol and water.
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glycoconjugate
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A molecule that possesses covalently bound carbohydrate components (examples are glycoproteins and glycolipids)
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proteoglycan
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A large molecule containing large numbers of glycoaminoglycan chains linked to a core protein molecule
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glycoprotein
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A conjugated protein in which carbohydrate molecules are covalently bound to amino acid side chains
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lectin
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A carbohydrate binding protein
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look at
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14a. Ribonuclease B is an example of a glycoprotein
14b. Each proteinglycan contains glycoaminoglycans such as chonfroitin sulfate and dermatan sulfate which are linked to a core protein via glycosidic linkages 14c. Lactose is an example of a disaccharide 14d. Heparin is a glycosaminoglycans |
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heteroglycans
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Heteroglycans are made up of more than one type of monosaccharide residue but homoglycans have only one. Examples of homoglycans and heteroglycans are startch and hyaluronic acid.
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lookat
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Glycogen stores glucose
20b. Glycosaminoglycans are components of proteoglycans 20c. Glycoconjugates may serve as membrane receptors 20d. Proteoglycans provide strength, support, and elasticity to tissue 20e. Hormones such as FSH and enzymes such as RNase are glycoproteins 20f. Polysaccharides, or glycans, play important roles in the storage of carbohydrate (starch and glycogen) and the structure of plants (cellulose) |
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look at
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Carboxylate, sulfate and hydroxyl groups bind large amounts of water.
21b. Hydrogen bonding is the primary type of bonding between water and glycosaminoglycans. |
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glycoproteins
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. In glycoproteins the three amino acids that the carbohydrate groups are most frequently linked to are the amide nitrogen of asparagine and the hydrozxyl oxygen of serine and threonine residues. The glycan is linked by amide bonds.
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proteoglycans
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Proteoglycans are extremely large molecules that contain a large number of glycoaminoglycan chains linked to a core protein. They are found primarily in extracellular fluids where their high carbohydrate content allows them to bind large amounts of water. Glycoproteins are conjugated proteins in which the prosthetic groups are carbohydrate molecules. The carbohydrate groups stabilize the molecule through hydrogen bonding, protecting the molecule from denaturation, or shielding the protein from hydrolysis. The carbohydrate groups on the glycoproteins on the surface of cells play an important role in a variety of recognition phenomena.
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pathogenic organisms
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Pathogenic organisms bind to the milk oligosaccharides instead of the oligosaccharides on the surface of the infant’s intestinal cells, thus preventing infections.
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sulfate groups
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The sulfate group has several negatively charged oxygens that are capable of hydrogen binding. Conjugation of sulfate with the hydrophobic molecule enhances solubility because of hydrogen bonding between the sulfate oxygens and water molecules in tissue fluids.
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thermodynamics
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The study of the heat and energy transformation in a chemical reaction
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bioenergentics
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Study of energy transformations in living organisms
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enthalpy
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– A measure of the heat evolved during a reaction
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entrophy
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A measure of the disorder during a reaction
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free energy
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A measure of the tendency of a reaction to occur
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work
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physical change caused by a change in energy
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exothermic and endothermic reactions
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exothermic- A reaction that releases heat
2c. Endothermic Reaction – A reaction that requires anenergy input |
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isothermic reaction
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reaction that has no heat exchanged with the surroundings
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spontaneous process
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Reactions that occur with the release of energy
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exergonic reaction
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A reaction that spontaneously goes to completion as written; the standard free energy change is negative, and the equilibrium constant is greater than 1
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endergonic reaction
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A reaction that does not spontaneously go to completion; the standard free energy change is positive and the equilibrium constant is less than 1
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phosphoryl group transfer potential
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The tendency of a phosphorylated molecule to undergo hydrolysis
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phosphoanhydride bond
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A type of high-energy bond formed between two phosphate groups that is present in ATP
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redox reaction
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Oxidation-reduction reaction where electrons are transferred from an electron donor to an electron acceptor
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resonance hybrid
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Occurs when a molecule has two or more alternative structures that differ only in the position of electrons
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electron donor
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A molecule that provides electrons to an oxidation-reduction reaction
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coupled reactions
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. Reactions are coupled when the product of one is a reactant in another. The principal involved in this phenomenon is the principal of coupled reactions.
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