Korean, Edit

Chapter 3. Cell and Material Metabolism

Higher category : 【Biology】 Biology Index 

1. Nutrient

2. Enzyme

3. Organic chemical reaction

4. Transport through membrane

5. Body fat and health

a. Protein lyase mechanism

b. Relationship between enzyme and substrate

c. Allosteric regulation

1. Nutrient

⑴ Classification of nutrients

① Nutrient : Active ingredient that acts nutritionally in the body among food ingredients

○ Essential Nutrients : Substances that cannot be synthesized directly

② Macronutrient vs. Micronutrient

○ Macronutrient : Much required water, carbohydrates, protein, fat

○ Micronutrients : Trace amounts required vitamins, minerals

③ Three major nutrients vs eutrophic nutrients

○ Three major nutrients : Carbohydrates, Proteins and Fats Used as Energy Sources

○ Eutrophic : It is not used as an energy source, but vitamins, inorganic salts, and water

⑵ Water

① Role of water : Solvent, cell activity, transport (nutrient dispersion, waste removal), blood pressure and body temperature maintenance

② Body fluid distribution

③ Water loss : Adults need about 3 L of water each day (from food.5 L, 1 as a drink.5 L)

⑶ Carbohydrate

① Cell’s main energy source

○ 4 kcal / g. Energy is stored in chemical bonds

② Absorption rate : Monosaccharides & gt; Disaccharide & gt; Polysaccharides

③ Starch : Glucose polymer of plant

④ Glycogen : Glucose Polymers of Animals

○ Store carbohydrates in glycogen form in liver and muscle

○ Energy source exhausted in one day

⑤ Dietary Fiber (cellulose, etc.)

○ Colon digestive waste cleaning : Dietary fiber is not digested

○ Digestive waste : Bacteria, toxic substances, parasites, etc.

○ Intestinal cholesterol absorption, cancer risk 

○ The richest carbohydrate on earth

⑥ Detection reagent

○ Starch : Iodine-potassium iodide aqueous solution, iodine reaction, purple

○ Glucose, fructose, maltose, etc. : Benedict Reaction, Yellow Red, Heating Required

⑷ Protein

① Cell’s major energy source, cell’s major components

○ 4 kcal / g, energy stored in chemical bonds (last source of bulwark)

② Polymer of 20 amino acids, amino acids linked by peptide bonds

③ Essential amino acids

○ Amino acids to be taken as food. 8 for adults and 10 for children

○ Valine, Leucine, Isoleucine, Methionine, Threonine, Lysine, Phenylalanine, Tryptophan, Histidine, Arginine

○ Animal protein : All essential amino acids vs vegetable protein : Rarely contains all essential amino acids

○ Amino acids are hydrophilic and therefore not stored and should be supplied daily

④ Complete protein

○ Proteins containing all essential amino acids : Meat, eggs

○ Plant protein : Not a complete protein, vegetarian only requires the combination of various ingredients

⑤ Detection reagent : Burette reaction, purple

⑸ Fat

① Major storage energy molecules, protection of critical organs, warming, famine preparedness

○ 9 kcal / g. Energy is stored in chemical bonds

○ Used carbohydrates stored as fat

② Glycerol + Fatty Acid (Hydrocarbon) Tail

③ Essential fatty acids : Unsaturated fatty acids that cannot be synthesized in the body

○ Linoleic acid, linolenic acid : Polyunsaturated Fatty Acids in Corn and Safflower Seed Oil. Phospholipids present in cell membranes

○ Omega-3, Omega-6 : Korean Wave Fish (Example : Unsaturated fatty acids of salmon, sardines) and flax seed oil→ Heart protection

④ Trans Fats (Transitional Fats)

○ Fats that are solidified by hydrogenating unsaturated fats

○ Example : Shortening, Margarine

○ Increased risk of heart disease and diabetes

○ WHO recommended amount : The percentage of trans fat in your calories is less than 1%

⑤ Detection reagent : Sudan III, scarlet

⑹ Vitamin

① Coenzyme action usually required for enzyme function→ Control metabolism, physiology

② Provitamin : Vitamins before they are still active

○ Example : Beta Carotene, Ergocalciferol

③ Water soluble vitamins

○ Overview

○ Possibility of deficiency because it is not consumed or stored as fresh vegetables during cooking

○ Food form: supplements packed with compressed tablets

○ Dissolved in body fluids such as blood, tissue fluid, etc

○ Easy to cause deficiency because it’s excreted through urine

○ Riboflavin (vitamin B2 ) : FAD, FMN

○ Niacin (vitamin B3) : NAD +, NADP

○ Biotin (vitamin B7)

○ Folic acid (vitamin B9)

○ Vitamin B12 : Works with Co ions, participates in nucleic acid synthesis and hematopoiesis, converts homocysteine to cysteine

○ Vitamin C : Important for collagen synthesis, increases intestinal iron absorption

○ Deficiency : Scurvy

○ 1^st. Vitamin C acts as a coenzyme of prolyl hydroxylase

○ 2^nd. prolyl hydroxylase converts prolin into hydro-prolin, which has a significant amount in collagen

○ 3^rd. hydro-prolin has strong binding force and performs various binding functions in ECM

④ Fat-soluble vitamins (A, D, E, K)

○ Fat-soluble vitamins are not easily released, so overdose problems

○ Example : Vitamins A and D are stored in the liver

○ Food form : Supplements Packed With Oil Gel Capsules

○ Vitamin A : Rhodopsin Ingredient

○ Vitamin D : Activation of calcium pump in the small intestine, the only vitamin that the body can synthesize under the sun→ Promote calcium absorption

○ Deficiency : Rickets

○ Vitamin E : Tocopherol Tocotrienol, Fat Antioxidant, Infertility Prevention

○ Vitamin K : Blood coagulation protein activation

○ Carboxylates Glutamic Acid Residues of Prothrombin During Blood Coagulation

⑺ Mineral : Simple minerals require as little as 1 mg to 2500 mg per day

① A substance that does not contain carbon

○ Example : Calcium, iron, magnesium, sodium

② It is water-soluble so it is lost when we boil

③ Main function of inorganic ion

○ Salt : Osmotic component of extracellular fluid, action potential

○ Hyperactivity : High blood pressure

○ Potassium : Osmotic component of intracellular fluid, repolarization of membrane, establishment of resting potential

○ Hyperactivity : Muscle weakness, paralysis, heart failure

○ Calcium : Extracellular, muscle contraction, intercellular binding, secondary signaling

○ Deficiency : Osteoporosis, dwarfism

○ Hyperactivity : Kidney stones

○ Magnesium : ATPase

○ Phosphoric Acid, Carbonic Acid : Hydrogen Buffer

○ Goat : Ions corresponding to inorganic cations

○ Hyperactivity : High blood pressure

⑻ Malnutrition

① Malnutrition

○ Calorie intake is caused by a continually low supply of chemical energy needed by the body

○ Stored glycogen, fat, and protein breakdown→ Reduced muscle size and protein deficiency in the brain

○ Example : In sub-Saharan Africa, where droughts, wars, and AIDS epidemic exist, about 200 million people cannot get enough nutrition

○ Example : Anorexia nervosa (obsessive compulsive fasting)

② Malnutrition

○ Store three major nutrients as glycogen or body fat when animals eat more food than energy needs

○ Important for hibernating animals

③ Malnutrition

○ Lack of one or more essential nutrients

○ Example 1. Vitamin A Deficiency→ Fixed by Beta Carotene Supply (Golden Rice)

○ Example 2. If you eat plants grown on soil that lacks phosphorus→ Herbivore bones easily break

○ Example 3. Diet not containing enough essential amino acids→ Protein deficiency

⑼ Assessment of Nutrient Needs

① Using humans for research purposes raises ethical issues

② Hemochromatosis : Genetic disease in which iron accumulates even without abnormal iron consumption

③ Epidemiology : To study health and disease at the collective level

○ Example : Folic acid intake significantly reduces neural tube defects that are fatal to fetal birth; Neural tube defects occur because the developing brain or spinal cord does not close

2. Enzyme

⑴ Metabolism : All chemical reactions in the body

① Gibbs Free Energy :  ΔH - TΔS < 0, the response is spontaneous

② Considered as ΔH ≒ ΔG in biology

○ Exothermic reaction : ΔH < 0, related to catabolism

○ Endothermic reaction : ΔH > 0, related to anabolism

③ Even if the reaction is spontaneous, if the activation energy (threshold energy) is too high, the reaction may be slow

④ Activation energy

○ Definition : Minimum energy required for reaction molecules to trigger chemical reactions

○ Lower activation energy increases the reaction rate by increasing the number of molecules that can react

○ Catalyst : It increases the reaction rate by lowering the activation energy in combination with the substrate

○ Enzyme : Biocatalyst

⑵ Characteristic

① Feature 1. Substrate specificity : The enzyme acts only on a specific substrate that conforms to its active site and conforms to the reaction catalyst.

○ Lock and key model : Model where the active site of the enzyme is completely consistent with the substrate

○ Induced fit model : The model that the enzyme turns into a completely complementary structure that fits the substrate when it is bound to the substrate.

○ 1^st. The shape of the substrate is approximately similar to the enzyme active site

○ 2^nd. When the substrate binds to the active site, the enzyme changes shape and the chemical bond is pressed.

○ 3^rd. Changes in shape break down substrates and release monomers

○ Isozyme (enzyme multiplicity)

○ Different enzymes involved in the same biochemical reaction

○ Have different characteristics depending on the cell that acts (eg : hexokinase, lactose dehydrogenase (LDH)

○ Feedback controlled by different end products, resulting in different enzymes depending on the end product type

② Feature 2. Recycle : The amount of enzyme before and after the reaction is the same

④ Feature 3. The enzyme only affects the reaction rate but does not affect the size of the reaction heat.

⑤ Feature 4. From common ancestors : When other organisms use the same enzymes 

⑵ Composition of enzymes

① Classification of enzyme : Divided into RNA enzyme (called ribozyme) and protein enzyme, commonly referred to as protein enzyme

② Active site : Sites that bind to the substrate

③ Apoenzyme : Protein parts that make up the enzyme

④ Cofactor : Nonprotein parts that make up enzymes. Attaches to the active site to complete the active site

○ Coenzyme : Organic molecules required for the activity of the enzyme

○ Example : Vitamin Derivatives, NAD+, FAD 

○ Inorganic ion : Metal elements such as Fe2+, Cu2+, Mg2+, Zn2+

○ Prosthetic group : Permanent binding due to the strong binding of enzymes to cofactors

○ Example : Hemoglobin heme group (organic compound containing Fe 2+ in porphyrin ring)

⑤ Holoenzyme : Enzyme that shows full activity by cofactor binding to main enzyme

⑥ Most hydrolytic enzymes, such as amylase, pepsin, and lypate, consist only of protein

⑶ Enzyme Catalytic Mechanism

① Acid-base catalysis

② Covalent catalysis

③ Metal ion catalysis

④ Electrostatic catalysis

⑤ Proximity and orientation effects

⑥ Differential binding of the transition state complex

⑷ Factors affecting the action of enzymes

① Factor 1. Substrate concentration

○ Related to Michaelis-Menten Equation

○ Initial reaction rate increases with increasing substrate concentration and then becomes constant after reaching a certain level

○ Once all the enzymes are saturated with the substrate, the initial reaction rate no longer increases with increasing substrate concentration.

② Factor 2. Temperature

○ As temperature increases, the number of molecules with kinetic energy above the activation energy increases, increasing the reaction rate.

○ The chemical reaction involving enzymes is the fastest at the optimum temperature at which the enzyme has the optimum conformation

○ When the temperature is above the optimum temperature, the protein is irreversibly denatured by heat, and the protein is not recovered even at a lower temperature

③ Factor 3. PH

○ The chemical reaction involving enzymes is the fastest at the optimum pH

○ The charged state of the amino acid residues that make up the enzyme depends on the change in the concentration of hydrogen ions, so if it is out of optimum pH, it changes the net charge of the protein, causing electrostatic repulsion and altering the conformation of the enzyme.

○ Example : Pepsin 1.5, catalace : 7.6, trypsin : 7.7, puma race : 7.8, ribonucleace : 7.8, Argenes : 9.7

④ Enzyme Reaction Rate Index

○ 1 unit of enzyme : Enzyme activity that can produce 1  mol of product in 1 minute

○ Enzyme activity = enzyme unit / amount of enzyme (ml)

⑸ Classification of enzyme : Regulated by IUPAC, also known as enzyme commission number

① EC1 : Oxidoreductase

○ A redox-mediated enzyme that transports hydrogen, oxygen, and electrons

○ Type 1. “Reactant + dehydrogenase” (Yes : lactose dehydrogenase, alcohol dehydrogenase)

② EC2 : Transferase

○ Transfer functional groups such as methyl, acyl and amino groups to other substances

○ Type 1. “trans + reactant + -ase” (Yes : Transaminase, acetyltransferase)

○ Type 2. “Reactant + -kinase” (Yes : Hexose kinase

③ EC3 : Hydrolase

○ Participate in hydrolysis and condensation

○ Type 1. “Reactant + -ase” (Yes : protease, peptidase)

④ EC4 : Lyase

○ Catalyze the addition or removal of atomic groups by cleaving C-C, C-O, C-N, C-S bonds, etc. of the substrate

○ Addition reaction is two substrate reaction, desorption reaction is one substrate reaction

○ EC4.4 : C-N Degrading Enzyme

○ EC4.5 : C-halogenase

○ EC4.6 : P-O Degrading Enzyme

○ Class 1. “Reactant + decarboxylase” (Yes : pyruvate decarboxylase)

⑤ EC5 : Isomerase

○ Enzymes that rearrange the structure of a substance

○ Type 1. “Reactant + isomerase” (Yes : phosphoglucose isomerase)

○ Type 2. “Reactant + mutase”

⑥ EC6 : Ligase

○ ATP is used to form new bonds between two materials

○ Type 1. “Reactant + ligase” (Yes : DNA ligase)

⑹ Michaelis-Menten Equation

⑺ Inhibitor : In vivo, there is an enzyme inhibitory mechanism to suppress feedback, but unlike the inhibitor, the reaction is reversible

① Irreversible inhibition

○ Example 1. Penicillin-A bacterium cell wall (peptidoglycan) transpeptidase inhibitor, potent because it has a semi-permanent covalent bond with the active site

○ Example 2. Sarin Gas

○ 1^st. Irreversibly binds to the active site of acetylcholine esterase

○ 2^nd. Acetylcholine 

○ 3^rd. Muscle spasms, pupil shrinkage, delirium, dyspnea

② Reversible inhibition : Competitive inhibition, anti-competitive inhibition, non-competitive inhibition

③ Competitive inhibition

○ Inhibits enzymatic reactions by competitively participating in enzymatic reactions over active sites such as substrates

○ Michaelis-Menten Equation (Reference⑹)

○ Does not alter the form of the active enzyme

○ Example : Ibuprofen, statin-HMG-CoA reductase, Ras phosphorylation of Gleevec-Bcl-abr, other antidepressants, antibiotics, insecticides, HIV protease

○ Reference. Ibuprofen : Inhibiting Prostaglandin Production

○ Example : Malonic Acid-Succinate Dehydrogenase : Succinic dehydrogenase oxidizes succinic acid, which inhibits the oxidation of succinic acid when malonic acid, a competitive inhibitor of succinic acid, binds to the active site of succinic acid dehydrogenase

④ Anticompetitive inhibition

○ Inhibitor binds to enzyme-substrate complex and inhibits enzymatic reaction

○ Michaelis-Menten Equation (Reference⑹)

⑤ Noncompetitive inhibitors

○ Inhibits the enzymatic reaction by binding to an allosteric site other than the active site, resulting in uncompetitive participation in the enzymatic reaction.

○ Michaelis-Menten Equation (Reference⑹)

○ Changes the form of active enzymes

⑻ Cooperative : Substrates already bound in the substrate enzyme to aid in the binding of other substrates

Reference. There is also voice cooperation but extremely rare

① Scheme : If there is co-operation, ESn is generated immediately after ES1 is generated, so it is not necessary to consider ES1, ···, ESn-1 

② Example : Oxygen Saturation of Hemoglobin

⑼ Enzyme Control Mechanism

① Control by suppressor (see. ⑹)

② Allosteric control (allosteric control)

○ A substrate is bound to an allosteric site of an enzyme to reduce the affinity of the enzyme

○ Does not completely block the reaction like an inhibitor

○ Allosteric regulation occurs in enzymes involved in irreversible reactions

○ Graph form

○ PFK-1 is an enzyme involved in the production of F-6 as F-1,6-bisphosphate

○ Because ATP is a substrate of PFK-1, PFK-1 is allosteric controlled by ATP

○ Graphs with ATP amount on the x-axis and PFK-1 activity on the y-axis show bell-shaped graphs

○ A representative example : Cooperative

③ Phosphate Control

④ Regulatory proteins

○ Example : NO synthase regulation of Ca²⁺-Calmodulin

⑽ Enzyme immobilization : Immobilizing enzymes in specific positions

① Entrapment (encapsulation) : Most widely used as physical enzyme immobilization method

○ porous hollow fiber

○ spun fiber

○ gel matrix

○ micro-capsule

② Combination : Chemical enzyme immobilization method, functional groups on the surface of carrier and period of action of enzyme

③ effective factor = reaction rate with diffusion limitation / reaction rate without diffusion limitation

○ How much better the reaction rate was by immobilizing the enzyme

○ Enzyme concentration → effective factor ↓ (meaning that the reaction occurs well because the concentration is high regardless of fixation) 

⑽ Enzyme Assay

① UV spectrometer

○ 260 nm UV spectrometer : Measure the absorbance of the nitrogen base of the nucleic acid

○ 280 nm UV spectrometer : Most typically used, measuring the absorbance of phenyl groups of Phe, Trp, Tyr

○ 340 nm spectrometer : NADH absorbance measurement

○ 405 nm, 570 nm spectrometer : Ninhydrin reacts with amino acids to produce purple products

○ 500 nm spectrometer : Carotenoid Absorbance Measurement

○ 560 nm spectrometer : Hemoglobin Absorbance Measurement

○ 680 nm, 700 nm spectrometer : Chlorophyll Absorbance Measurement

○ 840 nm, 870 nm spectromter : Photosynthetic bacteria : Absorption Measurement of Pigment Molecules

② Bradford method : Determination of the change in wavelength caused by Coomassie Blue G dye binding to protein

○ Advantages : Fast and simple dosing time

○ Disadvantages : Interference caused by other substances, and the degree of binding of dyes to proteins varies

③ Lowry method : Measurement based on reduction of copper ions by amide bonds in amino acids

○ Advantages : Little difference between proteins

○ Disadvantages : Preparation reagent, procedure complexity, interference by other substances 

○ Modified protocols such as BCA method (bicinchoninic acid method) and Peterson method

④ Biuret reaction

⑾ Example of enzyme

① Example 1. Glucose transporter (GLUT) : Glucose Transport in Cell Membranes

○ Characteristic : Bidirectional. Only type D glucose can be transported in the glucose carrier. 12 passes through the cell membrane

○ GLUT1 : Present in all cells. Km = 1 mM

○ GLUT2 : Liver, interest cells, small intestine. Km = 10-20 mM. Low sensitivity due to high glucose in the first place

○ GLUT3 : Present in the brain. Km = 1 mM. The brain has high energy demand, so high sensitivity

○ GLUT4 : Present in muscle, fat. Km = 5 to 10 mM. Conditional Expression by Insulin

○ GLUT5 : Fructose Carrier. Present in the small intestine

○ Insulin expresses GLUT4 in vesicles in muscle cells

○ GLUT4 is more sensitive than GLUT2, concentrating glucose into muscle and fat→ Decreased blood sugar

② Example 2. Lactose dehydrogenase (LDH)

○ Consists of 4 units of H (heat form) or M (muscle form)

○ All five kinds : H4, H3M, H2M2, HM3, M4 

○ Isoelectric point of H is 5.7, isoelectric point is 8.4

○ Muscle : pyruvic acid by muscle form LDH→ Lactic acid (since muscles are fermented by lactate)

○ Liver : Lactate by muscle form LDH→ Pyruvic acid (since the liver develops glucose new biosynthesis)

○ Heart : Lactate by heart form LDH→ Pyruvate (because the heart needs to use lactic acid as an energy source)

③ Example 3. Hexose kinase

○ hexokinase : Present in muscle, very high substrate affinity for glucose

○ hexokinase : Presence in liver, low substrate affinity for glucose

④ Example 4. Ethanol decomposition

⑤ Example 5. Lactose intolerance 

○ Lactose is well secreted in infants, but lacks as an adult

○ Lactose intolerance is poor in European countries  

○ Process : Lactase deficiency in the small intestine→ No digestion of lactose→ Bacteria break down lactic acid→ Causes of gas and diarrhea

3. Organic chemical reaction

⑴ Response index

① P:O ratio : The amount of ATP produced when one oxygen atom is reduced to water by oxidative phosphorylation at the ratio of pi and oxygen.

○ 2O₂ + 2H⁺ → H₂O

② Respiratory quotient (RQ) : Molar carbon dioxide generated / molar oxygen reacted

③ Oxygen transfer rate (OTR) : The rate at which oxygen in the air dissolves in the solution

④ Oxygen uptake rate (OUR) : Oxygen respiration rate of microorganisms contained in the unit amount of the culture solution

⑵ Calorie and metabolic rate

① Calorie : The energy needed to raise 1 g of water by 1 C, or kcal, also reduced to C

② Cells use the energy of nutrients to work and maintain body temperature

③ Metabolic rate : A measure of the rate of enzyme reaction in a living body

○ Recommended Daily Intake : Adult male average 2700 kcal / day, adult female average 2100 kcal / day

○ Basic metabolic rate (75%) : Energy consumption rate, thyroid hormone, etc.

○ Activity metabolic rate (25%) : Energy consumption rate per hour required for certain activities

④ Chemical reactions used as energy sources

○ C-C bonding : Long term energy storage

○ C-H bond : Long term energy storage

○ C-OH bond : Short term energy storage

4. Transport through membrane

⑴ Plasma Membrane and Fluid Mosaic Models

⑵ Membrane protein

① Integral membrane protein

○ Transmembrane protein. Membrane penetration is alpha helix structure

○ Example : channel protein, carrier protein, pump

○ Function : Enzymatic reactions (multiple if only one protruded), signal transduction

○ Pro and Gly do not form alpha helix and therefore cannot exist at the membrane penetration site

② Superficial proteins (peripheral membrane protein)

○ Form attached to cell membrane. Electrostatic attraction to the membrane

③ Hydropathy plot : Identify transmembrane areas

④ Simple separation experiments of intrinsic and soluble proteins (surface and soluble fractions)

○ 1^st. Physical method (e.G.destroying cell membrane parts by sonification

○ 2^nd. Centrifugation

○ 3^rd. Supernatant Soluble Protein

○ 4^th. Surfactant in the lower layer (e.G.membrane detergent can be added to obtain membrane protein

⑶ Transport protein

① Classification by energy use : Passive and Active Transport

○ If the molecule being transported is very large, it is not called active transport (see. ⑹)

② Classification by cotransportation

○ Single molecule transport : Aquaporin, glucose carriers (GluT), etc.

○ East Joint Carrier : Na+-glucose co-carrier, H⁺-sugar co-carrier

○ Reverse co-transportation : Na+-H⁺ exchange carrier, Na+-Ca²⁺ exchange carrier, G3P-pi exchange carrier, etc.

⑷ Passive transport : Diffusion due to concentration gradient, no energy used

① Simple diffusion : Molecular migration from high to low concentrations

○ Migration of small hydrophobic molecules through phospholipids

○ No energy needed

○ Continue until equilibrium is reached

② Promotion : Diffusion of Hydrophilic and Chargeable Materials Through Membrane Proteins

○ Channel (pore) proteins : Pathway through which hydrophilic molecules can migrate

○ Ion selective

○ Similar to simple diffusion, not saturated

○ Category 1. Dependency channel : Ligand dependent channel, voltage dependent channel, mechanical stimulus dependent channel

○ Ligand Dependent Channels : Acetylcholine receptor

○ Voltage-dependent channel : Action potential triggering channel

○ Mechanical stimulus dependency channels : Auditory hair cells, etc.

○ Category 2. Ionophore : Significantly increases the permeability of certain inorganic ions to the cell membrane

○ Example : H + ion channel (DNP), K + ion channel (valinomycin)

○ Carrier (Porter) Protein

○ 1000 times slower than the transport rate of channel proteins

○ Like the enzyme, the Michaelis-Menten equation can be established and saturated

○ Water is the only substance via both ion channels and carrier proteins

③ Osmosis : Free-H₂O diffuses from high concentration (low saline) to low concentration (high saline) in a semipermeable membrane that can pass only water

○ Formulation

○ Hypotonic solution : Solution lower than osmotic concentration inside cell, animal cell hemolysis, plant cell environment (swelling)

○ (Plant Cells) Absorption = Osmotic Pressure-Squeeze (provided bulge pressure 0)

○ (Plant cells) conditions where absorption = 0 or swelling = osmotic pressure : Swelling

○ Isotonic solution : Solutions such as osmolarity inside cells, animal cell environment, plant cell wilting

○ Osmotic concentration inside the cell = 0.9% = 0.3 M = 300 mOsmol

○ Hypertonic solution : Solution higher than osmotic concentration inside cells, animal cell contraction, plant cell protoplast separation

○ Aquaporins are channels in form but can be saturated unlike regular channel proteins

⑸ Active transport : Transport protein transports specific ions and molecules against electrochemical concentrations

① Characteristic

○ Carrier protein called pump involved : No active transport in channel form

○ Use ATP

○ One-way transport

② Pump : Transport proteins involved in active transport. Divided into P type, V type and F type

③ P-type pump : Decomposition of ATP to attach phosphate to the pump to modify the structure of the pump to transport material

○ Na+ / K+ Pump : Only present in animals. Pump Na+ 3 molecules out of cells and K+ 2 molecules into cells

○ Example : When glucose is absorbed in the small intestine

○ K+ pump : Present in plants, bacteria and fungi. Pumping hydrophilic nutrients such as sugar

○ H⁺ Pump (P Type) : Present in plants, bacteria and fungi. Air Transport of Sugar and Lactose

○ H⁺ / K+ Pump : Involved in the hydrochloric acid secretion of gastric parietal cells. Cl- is manual transport

○ Ca²⁺ pump : Used to store calcium in vesicles

④ V-type pump : Direct use of energy generated when ATP is broken down

○ H + Pump (Type V) : Make the lysosomes and vacuoles into an acidic environment

⑤ F-type pump : ATP synthase acts as a pump to pump H +

⑥ Direct active transport (primary active transport) : When transporting energy directly

⑦ Indirect active transport (secondary active transport) : When transporting using active transport of other materials

⑹ Intracellular uptake, extracellular excretion : Large molecules cannot be passively or actively transported

① Characteristic : Via ATP

② Extracytosis : Membrane vesicles fuse with cell membranes and release large molecules

③ Endocytosis : Follicles form around large molecules and carry into cells,④ To⑥Separated by

④ Phagocytosis (phagocytosis) : Actively absorbed through pseudopodia

⑤ Nerve cell action (inclusion, pinocytosis) : Absorb randomly by incorporating certain cell membranes

⑥ Receptor mediated endocytosis : Selective absorption by forming follicles with receptors bound to the substrate

○ Example 1. LDL receptor mediated intracellular uptake

○ Example 2. Transcytosis : Endothelial vesicles penetrate the membrane

○ Example 3. B cell receptor

○ 1^st. LDL binds to receptors and is entrapped in vesicles by receptor-mediated inclusion and enters cells

○ 2^nd. Adaptin, clathrin-coated pit, and dynamin involvement when membranes are incorporated into cells

○ Dinamin : Use GTP. Cutting role

○ Stripping : Adaptin, Clathrin Removal

○ 3^rd. Receptor vesicles bind early endosomes

○ 4^th. After the receptor and LDL are separated, the LDL moves to the initial endosomes

○ 5^th. Recycle : Receptor vesicles separate and migrate to cell membrane

○ 6^th. Early endosomes isolated from receptor vesicles bind to Golgi-derived primary lysosomal vesicles

○ 7^th. Become a secondary lysosomal vesicle (mature endosome) after binding

○ 8^th. Mature endosomes merge with mannose pathway to complete lysosomes

○ 9^th. Cholesterol isolation

5. Body fat and health

⑴ Health body fat evaluation

① Overweight : There is no definition

② Women demand more body fat than men for fertility

○ Female : 22% (12-32%)

○ Male : 14% (3 to 29%)

③ Larger bones, older body fat increase

④ Body weight indicator (BMI) : Weight (kg) (height (m)) 2, incomplete

○ Low weight : 18.Less than 5

○ Normal : 18.5 to 24.9

○ Overweight : 25.0 to 29.9

○ Obesity : More than 30

⑵ Obesity and Complications

① Obesity is affected by both lifestyle and heredity, causing complications

② Diabetes

○ Insulin : Beta-cells produced by the pancreas, glucose-promoting hormones of other cells

○ Type 1 Diabetes (Insulin Dependent) : Unrelated to obesity, genetically devoid of pancreatic beta cells, unable to produce insulin

○ Type 2 Diabetes (Insulin Independent) : Abnormal insulin response, obesity and association, usually in adults, controlled by diet and exercise

③ High blood pressure : High blood pressure

○ Systolic : Blood pressure when the heart contracts

○ Diastolic : Blood clots when the heart relaxes

○ Normal blood pressure : 120/80

○ High blood pressure : Continuously over 140/90

④ heart attack : Abrupt cardiac muscle blood flow blocked by coronary artery blockage

⑤ Stroke (seizure) : Cerebral artery blockage or rupture causes abrupt brain blood flow

⑶ Cholesterol

① Function : Cell membrane and steroid hormone production

② Carried by lipoproteins in the blood, accumulates in the arteries causing atherosclerosis

③ LDL (Low Density Lipoprotein) : Synthetic from liver, food→ Transport cholesterol to tissue

④ HDL (High Density Lipoprotein) : Group→ Transport cholesterol to the liver (for excretion in bile)

⑷ Appetite control disorders

① Loss of appetite

○ Self starvation, weight conscious eating disorders

○ Can cause myocardium and cause irregular beats

○ Stopping menstruation by blocking estrogens, risk of infertility

○ Increased risk of osteoporosis

② Appetite

○ Use laxative after binge eating

○ Risk of stomach rupture, problems with teeth and gums from stomach acid, dehydration

Input : 2015.6.25 10:01

Modify : 2019.2.16 09:45