Save
Busy. Please wait.
Log in with Clever
or

show password
Forgot Password?

Don't have an account?  Sign up 
Sign up using Clever
or

Username is available taken
show password


Make sure to remember your password. If you forget it there is no way for StudyStack to send you a reset link. You would need to create a new account.
Your email address is only used to allow you to reset your password. See our Privacy Policy and Terms of Service.


Already a StudyStack user? Log In

Reset Password
Enter the associated with your account, and we'll email you a link to reset your password.
focusNode
Didn't know it?
click below
 
Knew it?
click below
Don't Know
Remaining cards (0)
Know
0:00
Embed Code - If you would like this activity on your web page, copy the script below and paste it into your web page.

  Normal Size     Small Size show me how

CHE Exam 4

QuestionAnswer
Aldose is a monosaccharide with an aldehyde functional group
Ketose is a monosaccharide with a ketone functional group
D-glucose (most abundant and most important monosaccharide, comes from ripe fruit (grapes), also known as dextrose and blood sugar, primary energy source for cells, glucose in human blood range) ((70-100 mg)/ (100 mL blood))
D-galactose (called brain sugar, synthesized in mammary glands with glucose to produce lactose (milk sugar), 1. Also called brain sugar-part of brain and nerve tissue. 2. used to differentiate between blood types. 3. six membered cyclic form.)
D-fructose (biochemically most important Ketohexose, known as a fruit sugar or levulose, sweetest testing of all sugars, converted to glucose in the body, same calories/ (more sweetness per gram), found in fruit juices and honey, Honey 1:1 fructose to glucose)
D-ribose (Component of RNA and ATP, 1. part of RNA. 2. Part of ATP. 3. part of DNA. 4. Five membered cyclic form)
Haworth Structures (You can tell its BETA when the OH is pointing up in the same direction as CH2OH)
Anomers (Cyclic monosaccharides that differ only in the position of the substituents on the anomeric carbon atom)
5 Important reactions of Monosaccharides 1. Oxidation to acidic sugars 2. Reduction to sugar alcohols 3. Glycoside formation 4. Phosphate ester formation 5. Amino sugar formation
How do you turn a primary alcohol into a carboxylic acid? Oxidize a primary alcohol creating an aldehyde, then oxidize the aldehyde which creates a carboxylic acid)
How do you turn a aldehyde into a primary alcohol? Put an aldehyde through reduction
What is a sugar alcohol? an aldose that has been reduced to a hydroxyl group (H2 is the reducing agent), Ex. reduction of D-glucose to D-glucitol, Named by replacing the -ose ending of the monosaccharide with -itol, used as sweeteners in many sugar-free products, AKA alditols
Blood types .... are biochemical based on monosaccharides
What is a glycosidic linkage? The carbon-oxygen-carbon bond in disaccharides (this disaccharide bond occurs between the hemiacetal C atom -OH group of one monosaccharide and the -OH group of another monosaccharide)
What is malt sugar?? Common ingredient in baby foods and found in malted milk, germinated barely that has been baked and ground contains maltose (think beer)
Lactose (milk sugar, made up of 2 monosaccharides: galactose and glucose, lactose converted to lactic acid by bacteria cause the souring of milk, lactose intolerance= the inability to digest hydrolyze lactose) (Lactose + H2O__Lactase__> glucose + galactose)
Sucrose Table sugar, comes from sugar cane and sugar beets, made up from glucose and fructose, Sucrose CANNOT: form an open chain or be oxidized, react with benedicts reagent [nonreducing sugar], (D-sucrose + H2O __H+ or Sucrase__> D-glucose +D-fructose)
Polysaccharides polymers of many monosaccharides linked together, differ in the type of links between monosaccharides, differ in the type of monosaccharides in the polymer, differ by the amount of branching in the polymer [NOT SWEET]
Starch Contains only glucose molecules. 2 different starches: Amylose- 15%-20% of starch, amylopectin- 80%-85% of starch. (human can hydrolyze alpha linkage but not beta linkage)
Amylose alpha-D-glucos molecules, alpha-1,4 glycosidic bonds. Alpha= C-O-C ( V shaped linkage )
Amylopectin Branched polymer of alpha-D-glucose molecules, alpha-1,4-glycosidic bonds between the glucose molecules, has alpha- 1,6 bonds to branches
Glycogen (maintains the blood level of glucose and provides energy between meals) Contains only glucose. Animal starch. Storage form for glucose. Stored in liver and muscle tissue. ( Glucose <__Glycogenesis__> Glycogen Glycogenolysis
Cellulose Most abundant polysaccharide. Made up of glucose. Structural component of cell walls of plants has Beta(1-4) glycosidic bond. Humans can't digest cellulose. Dietary fiber ("bulk") in food- Readily absorbs H2O & results in softer stools. (20-35 g daily des
Chitin Polysaccharide that gives arthropods theri rigid exoskeletons (crabs, lobsters, shrimp, insects etc.) Similar to cellulose in both function and structure
Mucopolysaccharides occurs in connective tissue in joints of humans and animals. Primary function is as a lubricant for joint movement
Homopolysaccharides 1 type of monosaccharide monomer
Heteropolysaccharides more than 1 type of monosaccharide monomer
Hyaluronic acid Highly viscous- serve as lubricants in the fluid of joints and part vitreous humor of the eye
Heparin an anticoagulant- prevents blood clots
Enzymes proteins that catalyze nearly all the chemical reactions taking place in the cells of the body (they are biochemical catalysts) ( they increase the rate of reactions by lowering the energy of activation) (most are globular proteins (soluble in H2O))
Yeast contains an enzyme used to speed up the decomposition of glucose to produce CO2 and ethanol in bread, wine, etc.
Simple enzyme Enzyme composed only of protein (amino acid chains)
Conjugated enzyme Enzyme that has non-protein and protein parts (derived from dietary vitamins) ( they contain vitamins as part of their structures)
Cofactor Non-protein part of conjugated enzyme. a. Metal ions: Zn2+, Fe3+, Mg2+ b. Coenzyme: small molecules
Naming of enzymes Suffix -ase identifies as an enzyme. Some of the digestive enzymes have -in at the end (Ex. pepsin, trypsin, and chymotrysin)
Six major classes of reactions 1. Oxidoreductase Oxidation reduction
Six major classes of reactions 2. transferase transfer of functional group from one molecule to another
Six major classes of reactions 3. hydrolase addition of water molecule
Six major classes of reactions 4. lyase addition or removal of a group to a double bond
Six major classes of reactions 5. isomerase rearrangement of functional group within a molecule
Six major classes of reactions 6. ligase bonding together 2 molecules into one
Substrate Reactant in an enzyme-catalyzed reaction (substance upon the enzyme "acts")
Enzyme active site the small part of the enzyme structure where the reaction occurs
lock-and Key model fixed, rigid geometrical conformation. Only substrates with a complementary geometry can be accommodated at the site
Induced-fit model (how a hand fits in a glove) flexible active site that adapt to the substrate
Enzyme specifity the limitation of an enzyme to catalyze one specific reaction with one specific substrate
1. absolute specifity enzyme-urease catalyzes only the hydrolysis of urea, but no other amides
2. stereochemical specifity glucose oxidase oxidizes only D-glucose not L-glucose
3. group specifity act only on molecules that have a specific functional group
4. linkage specifity enzyme will act on a particular type of chemical bond, rest of the molecular structure is not considered
Factors that affect enzyme activity 1. optimum temp. 2. optimum pH 3. substrate concentration (turn over number - at optimum conditions- the # of substrates transformed per minute by one molecule) 4. enzyme concentration
Enzyme inhibitor substance that slow or stops an enzyme reaction by binding to it
Competitive enzyme inhibitor has a chemical structure and polarity that is similar to that of the substrate. Competes with the substrate for the active site. Has its effect reversed by increasing substrate concentration
Enzymes are used to diagnose certain diseases such as Blood urea nitrogen levels (BUN)- common clinical lab procedure. high urea levels in the blood indicate kidney malfunction. AND After a heart attack, dead muscle cells dump their enzyme- creatine phosphokinase (CPK)
Non-competitive enzyme inhibitor decreases enzyme activity by binding to a site on an enzyme other than the active site. Causes a change in the structure of the enzyme. Prevents the catalystic groups at the active site from properly effecting their catalyzing action.
Irreversible enzyme inhibitor Inactivates enzymes by forming a strong covalent bond to amino acid side-chain group with the enzymes active site. Doesn't have a structure similar to that of the enzymes normal substrate. increasing substrate concentration does not reverse the inhibition
Properties of allosteric enzymes Have quaternary structure. Composed of two or more protein subunits. Have at least two kinds of binding sites (substrate & Regulator binding sites). Active & regulatory binding sites are distinct from each other in both location and shape
Effects of + and - Regulators on an allosteric enzyme Binding of molecules at the regulatory site causes changes in the overall 3-dimensional structure of the enzyme. Binding of a + regulator increases enzyme activity. Binding of a - regulator decreases enzyme activity
Antibiotic substance that kill bacteria or inhibits their growth
Absorbic acid (Vitamin C) simplest Required in collagen synthesis and healing of wounds. Found in blueberries, citrus fruits, strawberries, tomatoes. Deficiencies are scurvy, weakened connective tissue, slow-healing wounds and anemia. It is the simplest in structure of all the 13 vitamins
Thiamin (Vitamin B1) Found in liver, yeasts, whole grain bread. Deficiencies lead to beriberi
Biotin (Vitamin B7) Found in liver, yeasts, nuts, eggs. Deficiencies include dermatitis, loss of hair, fatigue, and anemia
Riboflavin (Vitamin B2) Found in beef, liver, chicken, eggs, dairy foods. Deficiencies lead to dermatitis.
Niacin (Vitamin B3) Found in chicken, beef, fish. Deficiencies can result in dermatitis, muscle fatigue, and loss of appetite
Pantothenic (Vitamin B5) Found in salmon, beef, liver, eggs, fresh vegies. Deficiencies can result in fatigue, retarded growth, cramps and anemia
Cobalamin (vitamin B12) Found in liver, beef, kidney, fish, milk. Deficiencies are pernicious anemia, nerve damage, and malformed red blood cells
Folic acid (Vitamin B9) Deficiencies are abnormal red blood cells, anemia and poor growth. The absensence of folic acid increases the possibilty of a neural tube defect (a defecet in the development of the spinal cord) Pregnant women need to take this.
Pyridoxine (Vitamin B6) Found in mwat, liver, fish, nuts, and spinach. Deficiencies may lead to dermatitis, fatigue and anemia
Fat soluble vitamins Vitamins A, D, E, and K. Important in vision, bone formation, antioxidants, and blood clotting
Retinol (Vitamin A) Major funtions: 1. vision. 2. regulating cell defferentiation. 3. maintenance of the health of epithelial tissues. 4. reproduction and growth. Derived from Beta-carotene
Cholecalciferol (Vitamin D) Sunshine vitamin. D3- produce by ultraviolet light. D2- produced from plant sterol
Tocopherol (Vitamin E) Is an antioxidant in cells. Is found in whole grains and vegies. Has an RDA of 15 mg. Deficiencies are hemolysis and anemia. 4 Forms: 1. alpha- 2. Beta- 3. delta- 4. gamma-tocopherol. Plant oils, green leafy vegies and whole grain are good sources
Menaquinone (Vitamin K) essential in the blood-clotting process. Deficiciencies are prolonged bleeding time and bruising.
Water soluble vitamins Vitamin C, Thiamin, Riboflavin, Niacin, Pantothenic acid, Vitamin B6, Biotin, Folate, Vitamin B12
Lipids an organic molecule found in living organisms that is insoluble (or only sparingly soluble) in water but soluble in non-polar organic solvents
Water solubility short chain fatty acids have some solubility where as long chain fatty acids are insoluble
Five categories of Lipids: 1. energy storage- triacylglycerols. 2. membrane- phospholipids, sphingoglycolipids, and cholesterol. 3. emulsification- bile acids. 4. messenger- steroid hormones and eicosanoids. 5. protective coating- biological waxes
fatty acids naturally occurring monocarboxylic acid
polyunsaturated fatty acid a fatty acid with a carbon chain in which two or more carbon-carbon double bonds are present. Up to six double bonds are found biochemically important polyunsaturated fatty acids
Omega 3 fatty acid (mostly fish oils) unsaturated with a double bond, 3 carbonds from -CH3 (methyl) at the end of the chain
Omega 6 fatty acid (Vegie oils) unsaturated with a double bond, 6 carbonds from -CH3 (methyl) at the end of the chain
Nutritionally important Omega 3 and 6 fatty acids Linolenic acid- Omega 3 and Linoleic- Omega 6
Linoleic acid deficiency Skin redness, infections and dehydration, liver abnormalities, children need it the most, and human milk has more than cow milk
Essential fatty acids fatty acids needed by the body from diet source. Body cannot synthesize from other substances
Fat substitutes (Simplesse and olestra) composed of 6-8 long chain fatty acids attached by ester links to a sucrose (not glycerol) molecule
Triacylglycerol lipid formed by esterfication of 3 fatty acids to a glycerol
Simple triacylglycerols 3 identical fatty acids are esterfied
Mixed triacylglycerols a triester formed from the esterfication of glycerol with more than one kind of fatty acid
Physical state of triacylglycerols 1. fats: a)predominantly saturated b) solids or semisolids at room temp.. 2. Oils: a) predominantly unsaturated b)liquids at room temp.
Saturated fats bad fats
monounsaturated fats good fats
trans-monounsaturated fats bad fats
polyunsaturated fats good and bad fats. Omega 3 and 6 are good fats
Hydrogenation 1. addition of hydrogen across double (=) bond- increases degree of saturation 2. Many food products are produced by partial hydrogenation of oils and fats
Reactions of triacylglycerols 1. Hydrolysis- in the body 2. Saponification- making of soap 3. Hydrogenation- + Hydrogen to unsaturated triacylglycerols to increase their saturation 4. oxidation- breaks the carbon carbon bonds and forms smaller molecules.
Phospholipid contains one or more fatty acids and a phosphate group (most abundant type of membrane lipids)
Glycerophospholipid contains two fatty acids and phosphate group esterified to a glycerol molecule and an alcohol esterified to the phosphate group
Sphingophospholipids one fatty acid, one phosphate group with an alcohol group attached to the phosphate group
Sphingoglycolipids contains both a fatty acid and a carbohydrate component
Cholesterol 3rd major type of membrane lipid. Is an all cell membrane. It combines with proteins to form a lipoproteins
Lipoproteins carry cholesterol in the body
LDL (low density lipoproteins) Bad cholesterol. from liver to tissues
HDL (High density lipoproteins) Good cholesterol. from tissues back to liver
cell membrane lipid based structure that separates the aqueous part of the cell interior from the exterior
lipid bilayer two layer thick structure of phospholipids and glycolipids
Passive transport substances move across a cell membrane without using cell energy ( higher concentration to lower concentration)
Facilitated transport substances move across the cell membrane with the sid of membrane proteins without using cell energy (higher concentration to lower concentration)
Active Transport uses cell energy to pump membrane proteins to carry substances across the membrane (LOWER CONCENTRATION TO HIGHER CONCENTRATION)
Emulsifier disperses and stabilizes water-insoluble substancesas colloidal particles in an aqueous solution
Bile acid cholesterol derivative that functions as an emulsifying agent. It makes lipids soluble in aqueous solutions (digestive tract)
Bile Fluid containing bile acid secreted from the liver stored in the gallbladder
Messenger lipids Hormones and steroid hormones
Adrenocorticoid hormones produced from the adrenal glands located on top of each kidney. 28 different hormones have been isolated from the adrenal glands cortex.
Two types of adrenocorticoid hormones: 1. mineralocorticoid- control balance of Na+ and K+ ions in the cells. 2. glucocorticoid- control glucose metabolism and counteract inflammation
Aldosterone which regulates electrolytes and water balance by the kidneys
Cortisol released under stress to increase blood sugar and regulate carbohydrate, fat, and protein metabolism
Prednisone A synthetic corticosteroid, derived from cortisone, used for reducing inflammation, treating asthma, and rheumatoid arthritis
Eicosanoid oxygenated C20 fatty acid derivative that function as messengers
Physical effects of eicosanoids 1. inflammatory response, a normal response to tissue damage 2. production of pain and fever 3. regulation of bp 4. induction of blood clotting 5. control or rep. functions such as induction of labor. 6. regulation of sleep/wake cycle
Prostaglandins regulates many functions in body- C20-fatty-acid derivative containing cyclopentane ring and oxygen containing functional groups.
Thromboxane's C20-fatty-acid derivative containing a cyclic ether ring and oxygen containing functional groups. promote platelet aggregation
Leukotrienes found in white blood cells. Leukotrienes: C20-fatty-acid derivative containing 3 conjugated double bonds and hydroxy groups
Biological waxes a lipid with a monoester of long chain fatty acid and a long chain alcohol
Properties of biological waxes water-insoluble and water repellant because of long nonpolar hydrocarbon chains. humans and animals secrete biological waxes from skin glands
Function of biological waxes 1. prot. hair and skin 2. impart water repellency to animal fur 3. birds keep their feathers water repellent and help minimize loss of body heat 4. plants coat their leaves with a thin layer of biological waxes to prevent excess evap. of H2O
Type of fatty acid lipid Carnauba biological wax from the Brazilian palm tree
Type of fatty acid lipid Lanolin mixture of biological wax from sheep wool
Type of fatty acid lipid BHA butylated hydroxyantoluene
Type of fatty acid lipid BHT butylated hydroxytoluene
Protein biochemical polymer of monomer units of amino acids
amino acids molecule containing both an amino -NH2 and a carboxyl -COOH group
Standard amino acid one of 20 alpha- amino acids found in proteins normally
Cysteine the only standard amino acid with a sulfhydryl group (-SH group)
Nonpolar amino acid 1 amine group and 1 carboxyl group with nonpolar side chain
polar neutral amino acid 1 amine group and 1 carboxyl group with polar side chain, but nuetral
Polar acidic amino acid 1 amine group and 2 carboxyl group with side chain containing 2nd -COOH group
Polar basic amino acid 2 amine groups and 1 carboxyl group with side chain containing 2nd amine group
Achiral four different groups are attached to the alpha-carbon atom in all of the standard amino acids except glycin
glycin R-group is hydrogen
Essential amino acid needed by the human body, but must come from dietary sources
10 essential amino acids arginine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, valine
Soy has all the essential amino acids
simple proteins a protein in which only amino acid residues are present
conjugated protein a protein that has one or more non-amino acid group present in its structure
prosthetic groups (non-amino acid components) may be organic or inorganic
insulin the 1st to have its order of amino acids determined
Covalent disulfide bonds strongest
3 types pf proteins 1. membrane 2. fibrous 3. globular
fibrous protein polypeptide chains arranged in long strands or sheets (insoluble)
Keratins found in wool, feathers, hooves, silk, hair, and fingernails
collagens found in tendons, bone and other connective tissue (most abundant)
elastins found in blood vessels and ligaments
myosin found in muscle fissure
fibrin found in blood clots
globular protein polypeptide chains are folded into spherical or globular proteins (soluble)
Myoglobin involved in O2 transport in muscles
Hemoglobin Involved in O2 transport in blood
Transferring involved in iron transport in blood
Immunoglobin involved in immune system responses
Protein functions 1. catalytic 2. defense 3. transport 4. messenger 5. contractile 6. structural 7. transmembrane 8. storage 9. regulatory 10. nutrients
protein denaturation partial or complete disorganization of a proteins tertiary structure
glycoprotein protein that contains carbohydrates in addition to amino acids
antigen foreign substance in the body bacterium or virus
Created by: leah.flippin
Popular Chemistry sets

 

 



Voices

Use these flashcards to help memorize information. Look at the large card and try to recall what is on the other side. Then click the card to flip it. If you knew the answer, click the green Know box. Otherwise, click the red Don't know box.

When you've placed seven or more cards in the Don't know box, click "retry" to try those cards again.

If you've accidentally put the card in the wrong box, just click on the card to take it out of the box.

You can also use your keyboard to move the cards as follows:

If you are logged in to your account, this website will remember which cards you know and don't know so that they are in the same box the next time you log in.

When you need a break, try one of the other activities listed below the flashcards like Matching, Snowman, or Hungry Bug. Although it may feel like you're playing a game, your brain is still making more connections with the information to help you out.

To see how well you know the information, try the Quiz or Test activity.

Pass complete!
"Know" box contains:
Time elapsed:
Retries:
restart all cards