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104 Cards in this Set
- Front
- Back
Type of Lipids |
Esters- waxes, fats, oils, phospholipids *can be hydrolyzed Steroids- steroid nucleus of 4 fused carbon rings, *cannot be hydrolyzed |
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Physical properties of fatty acids |
physical properties- long, un-branched carbon chain with carboxylic acid group at one end-insoluble in waterUsually between 12-20 carbons (even numbers) |
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Phenols |
Functional group: Benzene ring bonded to an OH groupNaming: when there is a substituent other than the OH group, the benzene ring is numbered starting from carbon 1, which is the OH group (example: 3-Chlorophenol)Solubility of PhenolsSlightly soluble in water because of the OH groupWeak acid because the OH group ionizes slightly in waterVery corrosive, highly irritating to the skinCauses severe burns, ingestion is fatal |
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Oxidation of alcohol |
Oxidation is the addition of oxygen or the loss of hydrogenResult: an increase in the number of carbon-oxygen bondsOxidation of a primary alcohol produces an aldehydeOxidation of a secondary alcohol produces a ketoneTertiary alcohols do not oxidize readily because there is no hydrogen atom on the carbon bonded to the OH group |
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Saturated fatty acids |
contains only carbon-carbon single bonds—stack closely together. Higher melting point |
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Unsaturated fatty acids |
contains one or more carbon-carbon double bonds. So not stack closely together, Generally liquid oils at room temperature; less energy required to separate these molecules |
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Cis Vs Trans Isomers of Unsaturated fatty acids: |
Cis bonds are what causes the irregular shape. Causes the carbon chain to bend or kink giving an irregular shape. These cannot stack as closely as saturated fatty acids and have fewer interactions between carbon chains example, oleic acid |
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Prostoglandins |
can increase or lower blood pressure, stimulate contraction and relaxation in uterus, produce inflammation and pain after injury. Treating pain is based on inhibiting the enzymes that convert arachidonic acid to prostaglandins |
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Hydrogenation |
Adding H2 in presence of nickel turns unsaturated double bonds (lower melting point) into saturated single bonds (higher melting point) and each carbon gets an H. Number of carbons does not change and ester bonds do not change |
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Hydrolysis of triacylglycerol |
Triacylglycerol is hydrolyzed by water in presence of strong acid HCl or H2SO4, or digestive enzymes lipases. Products of ester bonds are glycerol and three fatty acids. |
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Soponification of triacylglycerol |
when fat is heated with a strong base. Triaclyglycerol (fat) + 3 sodium hydroxide (heat)-- 3 sodium salts of fatty acids (soap) + glycerol soluble |
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Purpose of cholesterol |
Used to synthesize steroid hormones. Liver synthesizes cholesterol for the body from fats carbs and proteins. Cholesterol reduces the flexibility of lipid bilayer and adds strength to cell membrane |
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LDL |
“bad cholesterol” carries cholesterol to tissues from the liver where used to synthesize cell membrane and steroid hormones. Excess amt causes plaque, which restricts blood flow to the heart |
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HDL |
“good cholesterol” picks up liver from tissues and cares to the liver where it can be converted to bile salts and eliminated from the body. |
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cell membrane |
separates the content of a cell from external fluids. Semipermeable so nutrients can enter and waste can leave. Has a nonpolar region (hydrocarbon tail), with two long fatty acid chains and a polar region head of phosphate and ionized amino acid. -Bilayer contains proteins/carbs/ and cholesterol (fluid mosaic) |
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3 types of transport through cell membrane: |
Diffusion- happens naturally moving from higher to lower concentrationsFacilitated transport: protein channels allow specific sizes to move throughActive transport: requires energy ions like K+ Na+ and Ca+ move against their concentration gradients |
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D& L Isomers |
all amino acids (except glycine) exist as D and L stereoisomers. Only L form can make protein. L group will have NH3+ group on the left. D amino acids are found in nature but not in proteins, we do not have the enzymes to break down D form of amino acids in our bodies. |
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Essential vs nonessential amino acids |
Essential- (9) must be obtained from proteins in diet Nonessential- (11) synthesized in the body |
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Essential fatty acids |
2 cannot be produced by the body The two primary EFAs are known as linoleic acid (omega-6) and alpha-linolenic acid (omega-3). |
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Peptide bond |
is an amide bond that forms when COO- group of one acid reacts with the NH3+ group of the next amino acid. O is removed from the carboxylate end of the first amino acid and two H atoms are removed from the ammonium end of the second amino acid, which produces water. Bond is always between the C & N |
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5 parts of tertiary structure |
hydrophobic interactions, hydrophilic interactions, salt bridges (ionic bonds), hydrogen bonds, and disulfide bonds (SH group) |
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which has higher melting point trans or cis bonds |
trans is higher melting point than cis |
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what is the reaction of palm oil with KOH |
saponification |
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reaction of glycerl trilinoleate from safflower oil with water and HCL |
Hydrolysis |
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why does glycine have no D or L form |
no stereocenter |
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secondary protein structure |
only affects alpha groups. has beta pleated sheats and alpha helix forms by hydrogen bonding between peptide bonds along the chain |
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primary protein structure |
p.p1 {margin: 0.0px 0.0px 0.0px 36.0px; text-indent: -31.5px; font: 12.0px 'Times New Roman'; color: #222d35; -webkit-text-stroke: #222d35}span.s1 {font-kerning: none}particular sequence of amino acids held together by peptide bonds, biological functions depend on this. |
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tertiary protein structure |
H+ bonding at side chains overall shape, polypeptide folds into a compact three-dimensional shape stabilized by interactions between R groups of amino acids to form a biologically active protein |
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quaternary structure |
2 or more protein subunits combine to form biologically active protein. Highest level of organization 2 or more polypeptide chains. Hemoglobin, a globular protein that carries oxygen in the blood, is one example. Made up of 4 polypeptide subunits alpha and beta chains + heme groups bound to oxygen. Ribbon model |
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denaturation |
occurs when there is a change that disrupts the interactions that stabilize secondary, tertiary, or quaternary structure NOT primary structure. Causes protein to unfold loss of overall shape (tertiary structure) no longer biologically active. Changes include: increasing temperature, changing ph, adding organic compounds, or mechanical agitation. |
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enzymes |
biological catalysts needed for most chemical reactions that take place in the body. Increases the reaction rate by lowering the activation energy required so less energy is needed |
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lock and key model |
describes the active site as rigid and non-flexible. The shape of the active size is like a lock and the substrate is a key that specifically fits that lock. –This does not include the flexibility of the tertiary shape of an enzyme |
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Induced fit model |
substrates fit into the active site by changing their size and shape to match those of the active site |
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hydrolysis of glycogen to yield glucose is catalyzed by the enzyme phosphorylase. caffeine inhibits phosphorylase as what kind of inhibitor |
non competitive inhibitor |
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transaminases |
transfer amino groups |
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isomerases |
rearrange to form isomers |
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does ethanol and methanol compete for the active site ? |
yes they are competitive inhibitors |
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organic chemistry |
the study of carbon compounds and the reactions they undergo |
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nonane properties |
liquid at room temperature, floats |
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what is the most important monosaccharide in the body and what is its major function |
glucose--provides energy to cells |
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what is the relationship between D-Ribose and L-Ribose |
enantiomers, mirror immages of each other |
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similarities and differences between amylose and amylopectin |
both store starch in plants amylose 20% amylopectin 80% Difference : amylose is unbranched, amylopectin is branched |
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similarities and diff between cellulose and glycogen |
both are polymers of glucose. cellulose--structural in plants with B glycosidic bonds. cannot be digested by humans glycogen--in liver and muscles of animals with alpha glycosidic bond |
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hydrogenation of alkene |
Alkene + H2 (catalyst PT, Ni, Pd) ---- Alkane *breaking double bonds, each carbon gets a H+ |
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reduction of aldehydes and ketones |
Aldehydes reduce to primary alcohols, Ketones reduce to secondary alcohols. H2 is added and bonds to carbon atoms, double bond breaks to single bond |
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protein |
large molecules made up of 20 different amino acids in a specific order that determines its characteristics and biological action. Protein provides structure in membrane, builds cartilage, transports oxygen in blood and muscle, defend body against infection and controls metabolic processes as hormones. |
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metabolism |
refers to all chemical reactions that provide energy and the substances required for continued cell growth. 2 types of metabolic reactions : anabolic and catabolic |
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catabolic reactions |
complex molecules broken into simpler ones with a release of energy |
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anabolic reactions |
utilizing energy available in the cell to build large molecules from simple ones |
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3 stages of metabolism |
1- catabolism begins with digestion where enzymes break down large molecules 2- digestion products broken down to yield 2&3 carbon compounds like pyruvate and acetyl-CoA3- major production of energy takes place in mitochondria as 2-carbon acetyl group is oxidized in citric acid cycle producing NAHD and FADH2----electrons from reduced forms transferred to electron transport chain to synthesize ATP |
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factors affecting enzyme activity |
Temperature—at low temps low amount of energy, at high temps over 50 Celsius for most, denatures. Optimal temp generally 37 degrees CPH- optimal generally around 7.4 except in stomach 2.0, above or below optimal can cause destruction of tertiary structureInhibitors- cause enzymes to loose catalytic activity, prevent active site binding with inhibitors some used to regulate enzymes |
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competitive inhibitor |
has a chemical structure and polarity similar to that of the substrate and competes with the substrate for the active site of the enzyme. Will occupy the active site so the substrate cannot bind, adding more substrate will reverse this |
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noncompetitive inhibitor |
structure does not resemble the substrate and does not compete for active site but instead binds to another site therefore changing the shape of the active site so substrate can no longer fit in. Can not be changed with addition of substrate but by chemical change that removes inhibitor |
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irreversible inhibitor |
often-toxic substances that destroy enzymes. Forms covalent bond with amino side groups within the active site, which prevents catalytic activity. Does not have similar shape to substrate |
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cholesterol structure and location |
Component of the cellular membrane, myelin sheath and brain and nerve tissue. Found in liver and bile salts, skin, adrenal gland. Structure: Steroid nucleus is for fused rings. Contains hydroxyl group **which determines its sterol classification**, methyl group and carbon chains |
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blood count |
men 4.7-6.1 million cells per mL women 4.2-5.4 hemocrit men 13-18 g/100mL women 15-18 g/100mL |
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digestion of food |
stage one of catabolism carbs begin in mouth lipids in small intestine protein in stomach and small intestine |
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electron transport and ox phosphorylation |
energy released during electron transport used to synthesize ATP from ADP and Pi a process called oxidative phos needs oxygen provides the most ATP enzymes in inner membrane |
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citric acid cycle |
1 turn produces 2 CO2, 3 NADH, and 3 H+, 1 FADH2, 1 GTP (ATP), 1 CoA 4 oxidation reactions take place 8 total reactions 8 enzymes |
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glycolysis |
oxidation of glucose anaerobic process no oxygen needed in glycolysis a 6 carbon glucose is broken down to 2 molecules 3-carbon pyruvate takes place in cytoplasm -net 2 ATP produced, 2 NADH |
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where does glycolysis take place |
cytoplasm |
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what is produced by glycolysis |
2 ATP and 2 NADH |
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coenzyme a |
prepare small acyl group like acetyl for reactions with enzymes |
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FAD |
oxidized Flavin Adenine Dinucleotide |
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NAD+ |
Oxidized Nicotinamide Adenine Dinucleotide |
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coenzymes in metabolic pathway |
NAD+, FAD, and Coenzyme A |
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The blood volume of an adult averages approx |
5 L |
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All of the following are true of RBC's except: a- biconcave disc shape b- life span of approx 120 days c- contains hemoglobin d- contain nuclei |
D- contain nuclei |
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blood proteins play an important part in A-blood clotting b-immunity c-maintenance of blood volume d- all the above |
D- all the above |
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The normal pH of the blood is about |
7.8 |
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Describe appearance of platelets and state major functions Why should they not be called cells? |
Appear as small discoid fragments of large multinucleoic cells called megakaryocytes -Essential for clotting, form temporary plug to prevent blood loss -They are only fragments of cells |
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total production from one glucose |
4 ATP 10 NADH 2 FADH2 |
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What is produced by glycolysis |
2 pyruvate, 2 NADH, 2 ATP |
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what is produced in 2 turns of citric acid cycle |
4 CO2, 6 NADH, 2 FADH2, 2 GTP, 24 ATP |
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what produces more atp per mole glucose or stearic acid |
stearic acid |
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what produces more atp per mole glucose or 2 pyruvate |
glucose |
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the fats and carbs metabolized by are bodies are eventually converted to one compound what is it and what is its purpose |
ATP, provides the energy to drive all the reactions in the cell |
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how many high energy phosphate bonds are in the ATP molecule |
2 |
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why are catabolic pathways long and complex |
allow for high degree of control over pathway |
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how many ATP produced by complete metabolism of glucose molecules in muscles |
32 |
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importance of FAD and NAD |
carriers of electron and hydrogen ions |
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where are enzymes of oxidative phos located |
inner membrane of mitochondria |
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muscle cramps are caused by |
accumulation of lactic acid |
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enzymes of glycolytic path are located in |
the cytosol |
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degradation of amino acids |
Happens in liver -alpha amino group removed to yield alpha keto acid which are converted to metabolic pathways. -Carbons from amino acids are used in citric acid cycle -most converted to urea *pyruvate can now enter citric acid cycle for production of energy |
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oxidation of unsaturated fatty acids |
energy from B-oxidation of unsaturated fatty acids is slightly less than energy from saturated but we assume the total ATP is same for both |
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ATP from fatty acid oxidation |
Stage 2 metabolism fatty acids udergo beta-oxidation removing 2 carbons from carboxyl end -results in acetyl-CoA and fatty acid shorter by 2 carbons Most energy produced from fatty acid in production of Acetyl-CoA that enters the citric acid cycle |
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function of hemoglobin |
protein that makes red blood cells red, binds easily and reversible with oxygen and carries through blood |
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functions of blood |
distribution, regulation, and protection -distributes oxygen, nutrients, transports metabolic waste -regulates body temp, pH, volume -protects from blood loss, and infectoin |
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formed elements |
erythrocytes, leukocytes, platelets |
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erythrocytes |
red blood cells, no nucleus, no mitochondria transports oxygen in capillaries of lungs and releases to tissues also transport carbon dioxide back to the lungs 97% hemoglobin |
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leukocytes |
white blood cells, only formed elements that are complete cells. less than 1% of blood volume help defend against disease, can go into blood vessels (diapedesis) |
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interstitial fluids |
solution that bathes and surrounds the tissue cells of multicellular animals. It is the main component of the extracellular fluid, which also includes plasma and transcellular fluid. |
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blood-brain barrier |
highly selective permeability barrier that separates the circulating blood from the brain extracellular fluid in the central nervous system (CNS). The blood–brain barrier is formed by brain endothelial cells, which are connected by tight junctions. |
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The angle in Methane between the carbon atom and a hydrogen atom was measured in the first Lab we did. What was that angle? |
109.5 |
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hydrogenation alkene |
Alkene + H2 (catalyst PT, Ni, Pd) ---- Alkane *breaking double bonds, each carbon gets a H+ |
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hydration alkene |
Alkene +H20 (catalyst H+ strong acid) --- Alcohol *breaks double bond and H bonds to one Carbon OH bonds to another carbon |
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naming and identifying ethers |
o in the middle of two groups naming Left of O, right of O then ether ending “Methyl Propyl Ether” |
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aldehyde and ketone name endings |
aldehydes: al ketones: one |
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which alcohol does not readily oxidize? |
tertiary |
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oxidation of alcohols |
Oxidation of Alcohols(increases the number of Carbon oxygen bonds): CH3-CH3---CH3-CH2-OH OR CH3-CH2-OH ---- CH3-CH=O |
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reduction of alcohols |
Reduction is the opposite of oxidation less bonds between carbon and oxygenCH3-CH=O --- CH3-CH2-OH OR CH3-CH2-OH----CH3-CH3 |
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oxidation of aldehydes and ketones |
aldehydes form carboxylic acid and ketones do not oxidize |
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oxidation of thiols |
forms a disulfide bond |