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Chemistry > gjiogd > Flashcards

gjiogd Flashcards

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1
Q

blood osmolality

A

increased: drink more, release antidiuretic

decreased: not thirsty, no antidiuretic

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2
Q

serum osmolality tests for

A

hydration
hyperglycemia
hypothalamus
ethylene glycol

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3
Q

ethylene glycol

A

kidney + liver try to metabolize -> toxic metabolites -> metabolic acidosis + nephrotoxosis from oxalate forming

TREATMENT: IV (often w sodium bicarbonate) of dilated ethanol competitive inhibitor

restores hydration, electrolytes, kidney function, excretes poison

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4
Q

fluid

A

crystalloid: lots small solutes, cross wall (hypo/iso), hydrating

colloid: large, don’t cross (iso), hold fluid

ISOTONIC: same osmolality as blood eg. 0.9% NaCl

HYPOTONIC: less osmolality than blood (more solutes inside than out)
- cell burst

HYPERTONIC: more osmolality than blood (more solutes outside)
- cell shrinks

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5
Q

solutes

A

electrolytes most common

organic molecules (proteins, phospholipids, cholesterol, triglycerides) large, less, uneven between compartments

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6
Q

diffusion

A

passive
- molecules from high -> low solute concentration
- depends on size, charge, and lipid solubility

FACILITATED
- carrier protein helps
eg. glucose -> muscle/fat

DIALYSIS
- blood circulated through fake kidney-> dialysate in opposite direction -> toxins go from blood to dialysate (lower concentration)

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7
Q

osmosis

A

the movement of water from low -> high solute concentration
- semipermeable membrane
eg. water in stomach -> bloodstream

OSMOTIC PRESSURE
- water comes in because more protein interstitial

ONCOTIC PRESSURE
- pressure difference between in/out, exerted to stop when equilibrium reached

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8
Q

filtration

A

hydrostatic pressure
- fluid moves out of capillaries based on pressure gradient (heartbeat)

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9
Q

membrane potential

A

changes in ion distribution on either side of membrane -> voltage

membrane selective: Na has a harder time moving in than K
- 2 K enter, 3 Na exit

eg. muscle cell contracting.

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10
Q

active transport ions

A

Na, K, Ca2, Mg2
- need ATP + carrier

either symport (same direction) or antiport

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11
Q

ion concentration maintains….

A

irritable cells (cells that create ATP through respiration)

eg. neurons, myofibrils

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12
Q

cytosis

A

nutrients in, waste out

ENDO: into cell
phago: eats solids by phagosome
pino: liquid through membrane folds
eg. small intestine
receptor mediated: cells w/specific proteins in their membrane
- ligabands bind -> coated pit vesicle
eg. insulin

EXO: out
- vesicles in ER and golgi move to cell surface, fuse to membrane, release contents extracellularly
eg. neurons -> acetylcholine.
eg. endothelial cells -> mucus
eg. mast cells -> histamine

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13
Q

carbs

A

glucose
- makes ATP through glycosis
- excess becomes glycogen, stored in liver or becomes fat

starch: rice, nuts, grains, roots

cellulose: all veg

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14
Q

fat

A

liver can convert b/w kinds

triglycerides/neutral fats
- 2x energy of carbs/proteins
- help absorb A D E K
- insulate, protect
- energy for muscle cells, skeletal cells, hepatocytes

fatty acids:
a. saturated: only single C bonds, max H
eg. meat, dairy

b. unsaturated: double bond Cs
eg. plant oils

essential:
linoleic, linolenic, arachidonic acid

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15
Q

protein

A

amino acids (NH2, COOH, R)
- all or nothing to make a protein
essential: taurine, arginine, glycine.

  1. complete: meat, eggs, dairy
  2. complement: legumes, grain

N balance: aminos not stored, used for protein or oxidized for energy or converted to carb/fat
- + = more protein in tissue than makes ATP
- - = protein breakdown more than in tissue
- BUN test (N packaged into urea in liver, excreted by kidney)

  • ruminants digest protein with microbes that improve the quality of protein
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16
Q

water

A

most important.
can also get through oxidizing protein/fat/carbs.
but this makes free radicals (A C E vitamins are antioxidants that disarm)

17
Q

vitamins

A

co-enzymes: keys that activate an enzyme
eg. riboflavin and niacin break down glucose

all from diet except
D (skin)
A (conversion to beta carotene)
K (intestine bacteria)

  1. water soluble
    - absorbed in GIT then peed out
    eg. C, B
  2. fat soluble
    - bind to ingesta, stored in body
    eg. A D E K [not stored]
18
Q

minerals

A

macro
micro
trace

19
Q

metabolism/catabolism

A

stage 1: GIT - hydrolysis
- protein -> amino
- carb -> glucose
- fats -> fatty acids + glycerol

stage 2: cytoplasm (anaerobic).
- pyruvic acid -> acetyl coA

stage 3: mitochondria (aerobic)
- ADP + Po4 = ATP

20
Q

anabolism

A

uses stored energy to make new molecules

metabolic turnover: constant manufacturing of new replacement molecules

energy storage: supplied by catabolism -> released when bonds break
eg. ATP, NADH, FADH2

dehydration synthesis: 2 things bond and extra H2O created
eg. poly = mono + mono
eg. fat = glycerol + fatty
eg. protein = amino + amino

21
Q

reactions

A
  1. redox: electrons removed from oxidation
    - reduction: gains e-, lost O, combines with H.
    - oxidation: lost e- and H, combined with O
  2. synthesis (anabolic)
  3. decomposition (catabolic)
  4. exchange: bonds broken and made
    eg. ATP transfers PO4 to glucose -> glucose-phosphate
22
Q

enzyme

A

act upon a substrate to create a product

co-factor: non-protein that completes for binding side
eg. iron, zinc, mg, K, ca

co-enzyme: nonprotein organic co-factors, often vitamins
- temporarily/permanently binds
eg. NAD, FAD, acetyl-coA

23
Q

enzyme activity factors

A
  1. enzyme concentration
  2. substrate concentration: levels out when saturated
  3. temperature: levels out when enzyme denatured
  4. pH: levels out at extremes (except pepsin which likes 1.5)
24
Q

clinical enzymes

A

only found in cell, in blood if damaged

alkaline phosphatase = liver/bone
amylase = pancreas
lipase = acute pancreatitis
alanine transaminase = hepatitis
aspartate transaminase = heart

assay on isozymes to pinpoint

25
Q

enzyme reversible inhibition

A

a. competitive
similar structure to normal substrate -> the more concentrated one winds
- reversed by increasing substrate concentration

eg. bacteria needs folic acid -> sulfanilamide resembles and competes -> folic acid stopped -> bacteria died

b. non-competitive
- no resemblance, binds elsewhere
- changes substrate’s shape so it doesn’t bind to normal substrate anymore
eg. isoleucine feedback inhibitor (end product inhibits earlier step)

26
Q

enzyme irreversible inhibition

A

covalent bond with functional group of enzyme -> inactivates it

eg. heavy metals combine to sulfyhydrl groups and cause neurological damage, chelating agents tightly hold on
eg. penicillin inhibits enzymes (transpeptidase) bacteria needs to build cell wall

27
Q

enzyme control mechanisms

A

zymogen: inactive precurose that is stored and released when needed
eg. prothrombin -> thrombin

genetic: adapt to environment, more enzymes made as needed

allosteric regulation: enzyme combines with modulator that either activates or inhibits -> shape changes
eg. isoleucine (modulator) binds to threonine deaminase and inhibits it -> total 5 enzyme reactions -> isoleucine levels are lowered, threonine deaminase active again -> more isoleucine made in response

Chemistry (5 decks)

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