GENERAL BIOLOGY 1  HYPOTONIC

- To Swell burst
WEEK 4
- The solution has lower solute
MITOSIS – 1 DIVISION – 2 DAUHTER CELLS concentration than the cell
MEIOSIS- 2 DIVSION – 4 DAUGHTER CELLS
HEMEOSTASIS – stable condition of
PASSIVE TRANSPORT organisms
-Equilibrium or balance inside the
 Movement of the materials across the cell
organisms.
membrane with cellular energy
CELL MEMBRANE – primary composed of
TYPES:
mixed proteins and lipids.
 PASSIVE TRANSPORT –no energy needed
FLUID MOSAIC MODEL (NICOLSON 1972)
- Higher to lower concentration
 ACTIVE TRANSPORT – energy needed  PHOSPOLIPIDS – major components of cell
membrane.
EXAMPLE OF PASSIVE TRANSPORT -lipid by layer
DIFFUSION – larger molecules pass through  HYDROPHILIC – water loving / attached o
the cell membrane through channels without water
using energy.  HYDROPHOBIC – water repelling /not
attracted to water
OUTSIDE & INSIDE OF THE CELL
AMPHIPATIC MOLECULES- it contains
FACILATED – unassisted movement of hydrophilic head and hydrophobic tail
solutes base in difference of concentration
from higher to lower concentration between Cell membrane lipids :
two regions.
EXAMPLES : OSMOSIS CHOLESTEROL – animal cell found only

- Help to keep cell membrane from

OSMOSIS – passage of water across a semi-
becoming stiff by preventing phospilipids
permeable membrane from the side of higher
from being too closely packed together.
to lower concentration
GLYCOLLIPIDS – carbohydrates sugar chain attached
TYPES OF TRANSPORT PROTEINS to them.
 CHANNEL- proteins embedded in the cell
membrane & have pore for materials to cross. IN ANIMAL CELLS, THE PLASMA
 CARRIER- proteins that change shape to MEMBRANE IS PRESENT IN THE
move material from one side of the OUTERMOST LAYER OF THE CELL AND IN
membrane to the other. PLANT CELL IT IS PRESENTJUST BENEATH
THE CELL WALL.
AQUAPORINS – water channel proteins
homeostasis. CELL MEMBRAIN PROTEINS:
Types of Solutions: 1. Integral proteins & Peripheral
 HYPERTONIC
-USED AS TUNNELS OR CHANNELS
- To shrink
- Higher concentration than cell
 UNIPORTER
 ISOTONIC
-flaccid and normal – unidirectional manner depending
-the solute the same inside and outside of on the concentration gradient.
the cell
 - Move materials from higher- lower
direction substance one at a time.
 SYMPORTER
- Transports different types of molecules
-the same direction SODIUM- POTASSIUM PUMP ( cat ions)
 ANTIPORTER – same time but different - Transporter that sits in the cell
direction.
membrane.

PREPHERAL PROTEINS / EXTRINSIC TYPES OF IONS :

- Receptors for hormones
 POSITIVE AND NEGATIVE
- Recognitions centers and antigens
PUMPS SODIUM (nat) – ions out of the cell
GLYCOPORINS
POTASSIUM (Kt) -into the cell.
- Proteins present in red blood cells
(Nat )– inside to outside - high to low
- Acts antigen determinant.
(Kt)- outside to inside -low to high

2- potassium ions ang napapasok, 2-3 ratio

GENERAL BIOLOGY
ang lalabas.
WEEK 5 SODIUM POTASSIUM IS IMPORTANT TO
BULK TRANSPORT – the movement of the cell MAINTAIN MEMBRANE POTENTIAL
membrane. MEMBRANE POTENTIAL-voltage across the
membrane
- It can take in any several forms
depending on the size the shape of the - To have a successful information of
substance carried in/out of the cell. neutrons- protons
TYPES : ENDOCYTOSIS – taking in different materials
 ENDOCYTIS TYPES :
 EXOCYTIS
PHAGOCYTOSIS – material that will be taking
ANKLE – it is the region where the foot and the solid
leg meet.
PINOCYTOSIS- taking liquid
CELL – it is the basic structural, functional, and
Amoeba- method for taking food
biological unit of all known organisms.
White blood cells- use phagocytosis to eat
TESTICLES/ TESTES – a pair sperm producing damaged cells
organs that maintain the health of the male
reproductive system. RECEPTOR- MEDIATED ENDOCYTOSIS

INTERNAL REGULATOR – these are proteins CLATHRIN – specialized proteins that are used
that react to changes within cell in coating the vesicles.

ACTIVE TRASPORT – process of transferring EXOCYTOSIS – release a substance may it be

substances into out and between cells using solid or liquid.
energy. PROTEIN PUMPS- changes their shape.
ATP ( ADONESINE TRIPHOSPHATE) –
undergoes a change in shape when it binds with
cells.
 GENERAL BIOLOGY INDUCE FIT MODEL
WEEK 6 (Daniel koshland 1958)
ENZYMES – 22 different digestive - active site is continuously
enzymes that our body produces. reshaped.
- Supports the presence of
- Proteins that catalyzed chemical
competitive and non-
reactions.
competitive inhibitor.
Examples: fruits, vegetables, other - -widely accepted other than lock
foods. and key model.

ACTIVATION ENERGY – energy DIFFERENCE OF COMPETITIVE & NON

needed to start a reaction. COMPETITIVE :
ACTIVE SITE – where substrate Competitive binds to the active site and
molecules bind and undergo prevent the substrate from binding them.
chemical reaction.
Non- Competitive Inhibitor binds to a
- Where substrate can be brought different site of the enzyme and doesn’t
together to react . block substrate binding. It causes changes
in the enzymes so that it can be no longer
SUBSTRATE -are the reactants of
catalyst the reaction efficiently.
enzymes catalyst reaction.
- It will not attached to active site
CATALYST – a substance that
(allosteric site) – allows non-
increases the rate of a chemical
competitive inhibitor attach.
reaction.
Enzyme name usually end in –ase
2 MODELS FOR ENZYME REACTIONS:
CLASSES OF ENZYMES :
1. LOCK AND KEY MODEL
2. INDUCED FIT MODEL 1. Oxidoreductase – catalyzes redox
reactions (e.g., cytochrome oxidase,
Lock And Key Model ( EMIL FISHER 1894)
lactate dehydrogenase)
- Highlights the specificity of the
2. Transferase – catalyzes transfer of
enzyme
functional groups (e.g., acetate
- Complementary shape.
kinase)
- does not support the
stabilization of the transition
stage that enzymes achieved.
 3. Hydrolase – splits chemical bonds - either change in the shape of
by addition of water (e.g. lipase and the active site or a complete
sucrase) denaturation of enzyme

4. Lyase – splits chemical bonds pH (either acidic or basic)

without using water (not a - also affects enzymatic acts.
hydrolysis reaction)
5. Isomerase – rearranges atoms
within a molecule (e.g., glucose- - The measure of hydrogen ions
phosphate isomerase) Hydroxides (OH)

6. Ligase – forms a chemical bond

between two atoms (e.g. acetyl CoA
synthetase, DNA ligase) Are changed particle which can interfere
with the bonds that holds the enzyme
together.
Enzymes play an essential role in INTERFERRENCE
controlling the chemical pathway.
– results in the change in the enzymes
Most enzymes are holoenzymes
ENZYMES WORKS BEST AT CERTAIN
IONIC CONDITION IN PH VAUES.
Consisting of protein portion /inactive SUBSTRATE CONCENTRATION – is equal
(apoenzymes) to enzyme concentration
-it will be only active if its cofactor will - Threshold point
bind to it .
Non protein portion (cofactor) EXAMPLE : increasing substrate
concentration will increase the
reaction but it will also reach this
Can be a metal ion or molecules
point where the enzymes will be
EX: fe, Cu Ex: NAD+ saturated and reach its maximum
possible rate.
REDUCTION OXIDATING
– using of electrons
The temperature at which the maximum
rate of reaction occurs is called the
enzyme’s optimum temperature.
Temperature