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Cell Biology

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Title: Cell Biology


1
Cell Biology
  • Achievement Standard 2.8
  • 90464

2
Cells
  • All living things are made up of 1 or more cells
  • Cells vary in shape but they are always small
  • Small size is due to difficulty in diffusing
    substances
  • Cells can be divided into 2 types
  • Prokaryotes
  • Eukaryotes

3
Cell Organelles
  • There are some organelles in cells that are
    present in both plant and animal cells, and
    others that are present only in one or the other
  • Cell wall (plant only)
  • Cell membrane
  • Cytoplasm
  • Nuclear membrane
  • Nucleus
  • Chromosomes
  • Mitochondria
  • Chloroplast (plant only)
  • Centriole
  • Vacuole
  • Ribosome
  • Endoplasmic reticulum (smooth and rough)
  • Lysosome
  • Golgi body

4
Nucleus contains inherited information The total
collection of genes located on chromosomes in the
nucleus has the complete instructions for
constructing a total organism.
Cytoplasm The nucleus controls cell metabolism
the many chemical reactions that keep the cell
alive and performing its designated role.
Structure of the nucleus
Nuclear pores are involved in the active
transport of substances into and out of the
nucleus
Nuclear membrane encloses the nucleus in
eukaryotic cells
Nucleolus is involved in the construction of
ribosomes
Chromosomes are made up of DNA and protein and
store the information for controlling the cell
5
  • Eukaryotes have two types of organelles with
    their own DNA
  • mitochondria
  • chloroplasts
  • The DNA of these organelles is replicated when
    the organelles are reproduced (independently of
    the DNA in the nucleus).

6
Unicellular Organisms
  • Unicellular organisms carryout all their life
    functions inside a single cell. While some of
    their organelles are the same as that of
    eukaryotes there are some that are found only in
    unicellular organisms. These are
  • Oral Groove Ciliated channel on one side of the
    cell where food particles are taken in
  • Anal Pore Specialised region of the cell
    surface where food vacuoles attach an rupture to
    the outside
  • Eyespots Is used in light detection and
    phototaxic responses
  • Contractile Vacuoles used to regulate the
    amount of water inside the organism by expelling
    it to the outside
  • Food Vacuole space that contained ingested food
    particles
  • Pseudopodia false legs to aid in ingestion of
    food particles

7
Unicellular Organisms cont..
  • As well as having specialised organelles, some of
    the cellular processes are significantly
    different to those of multicellular organisms.
  • Gas Exchange
  • This is usually by diffusion across the cell
    membrane. To increase efficiency, the organism
    is usually long and/or flat in shape increasing
    the surface area to volume ratio.
  • Ingestion and Feeding
  • All unicellular organisms that cannot
    photosynthesise must ingest small food particles
    as their food supply. Food particles cross the
    membrane by phagocytosis to form a food vacuole
    which is digested. Any indigestible material
    left in the food vacuole is discharged to the
    outside through the anal pore.
  • Some unicellular organisms do not have an oral
    groove so they use pseudopodia to engulf the food
    particles.
  • Excretion
  • In unicellular organisms, the main waste product
    formed is ammonia. This is very toxic so it must
    be diluted by large volumes of water before being
    excreted. Contractile vacuoles aid in the
    collection and removal of wastes.

8
Unicellular Organisms cont..
  • Water regulation
  • Since many unicellular organisms live in fresh
    water and are enclosed by semi-permeable
    membranes water is constantly moving into them.
    Contractile vacuoles work to collect and remove
    the water to ensure the cell does not burst.
  • Locomotion
  • For some unicellular organisms locomotion is
    achieved by the coordinated beating of cilia,
    others use flagella and Amoeba use the
    pseudopodia to move.
  • Responses to External Stimuli
  • Most movement is a response to changes in the
    protoplasmic contents of the organism. Some
    organisms have eyespots that detect the amount of
    visible light and trigger a phototaxic response.
  • Reproduction
  • This can be asexual via binary fission or, vary
    rarely, sexually through the exchange of genetic
    material

9
  • Bacteria have no membrane-bound organelles.
  • Cellular reactions occur on the inner surface of
    the cell membrane or in the cytoplasm.
  • Bacterial DNA is found in
  • One, large circular chromosome.
  • Several small chromosomal structures called
    plasmids.

Ribosomes
10
Cell Processes
11
Cell Membrane
  • Surrounds the cell and keeps it separate from the
    outside medium
  • Semi-permeable membrane that controls what goes
    in and out
  • In animal cells, it is the outside layer but in
    plants the cell wall surrounds it
  • Membrane is called a lipid bi-layer consisting of
    two hydrophillic heads on the outside and
    hydrophobic tails on the inside
  • The general structure is based on the fluid
    mosaic model.

12
Cell Transport
  • Materials such as ions, water, molecules and
    nutrients are transported within cells and in and
    out of cells by processes which are either
    passive or active.

13
Passive Transport
  • This does not require energy
  • It can be separated into 2 types
  • Diffusion
  • Osmosis

14
Diffusion
  • The net movement of particles from an area of
    high concentration to an area of low
    conentration.
  • Difference between the two areas is the
    concentration gradient
  • A large differencelarge gradientfaster
    diffusion
  • The rate of diffusion varies depending on
  • Size of molecules
  • Temperature of substance
  • State of matter
  • Concentration of chemicals
  • The cell membrane may contain proteins that help
    facilitate diffusion

15
Osmosis
  • The net movement of water from a high
    concentration to a low concentration through a
    semi-permeable membrane
  • Solution with not much water hypotonic
  • Solution with lots of water hypertonic
  • Solution with the same water concentration
    isotonic

16
Active Transport
  • Movement against a concentration gradient, ie
    from a low concentration to a high concentration
  • It requires energy so
  • Heat is given off
  • Oxygen is used up
  • CO2 produced
  • Glucose used up
  • Two main types
  • Endocytosis
  • Exocytosis

17
Endocytosis
  • Taking particles into a cell.
  • Engulfing a liquid pinocytosis
  • Engulfing a solid phagocytosis

18
Exocytosis
  • Occurs when vacuoles expel their contents to the
    outside

19
Amino Acids
  • Amino acids are linked together to form proteins.
  • All amino acids have the same general structure,
    but each type differs from the others by having a
    unique R group.
  • The R group is the variable part of the amino
    acid.
  • 20 different amino acids are commonly found in
    proteins.

20
Types of Amino Acid
  • Amino acids with different types of R groups
    have different chemical properties

21
Polypeptide Chains
  • Amino acids are liked together in long chains by
    the formation of peptide bonds.
  • Long chains of such amino acids are called
    polypeptide chains.

22
Protein Function
  • Proteins can be classified according to their
    functional role in an organism

Hemoglobin
Function Function Examples
Structural Forming the structural components of organs Collagen, keratin
Regulatory Regulating cellular function (hormones) Insulin, glucagon, adrenalin, human growth hormone, follicle stimulating hormone
Contractile Forming the contractile elements in muscles Myosin, actin
Immunological Functioning to combat invading microbes antibodies such as Gammaglobulin
Transport Acting as carrier molecules Hemoglobin, myoglobin
Catalytic Catalyzing metabolic reactions (enzymes) amylase, lipase, lactase, trypsin
23
Protein Structure
  • The production of a functional protein requires
    that the polypeptide chain assumes a precise
    structure comprising several levels
  • Primary structure The sequence of amino acids in
    a polypeptide chain.
  • Secondary structure The shape of the polypeptide
    chain (e.g. alpha-helix).
  • Tertiary structure The overall conformation
    (shape) of the polypeptide caused by folding.
  • Quaternary structure In some proteins, an
    additional level of organization groups separate
    polypeptide chains together to forma functional
    protein.

24
Enzymes
  • Enzymes are biological catalysts, regulating cell
    metabolism.
  • An enzyme acts on a molecule called the
    substrate.
  • Enzymes are specific for the reactions they
    catalyze.
  • Enzyme activity depends on the enzymes shape and
    its active site (the binding site for the
    substrate).
  • Enzymes are often named for the substrate on
    which they work, and sometimes include the suffix
    -ase
  • Lipase breaks down fats (lipids)
  • Amylase breaks down starch (amylose/amylopectin)
  • Lactase breaks down milk sugar (lactose)
  • Cholinesterase breaks down the neurotransmitter
    acetylcholine in the nervous system

25
Enzyme Structure
  • Ribonuclease S (right) is an enzyme that breaks
    up RNA molecules.
  • The red areas designate the active site and
    comprise certain amino acid 'R' groups.
  • The substrate (in this case, RNA) is drawn into
    the active site, putting the substrate molecule
    under stress, thereby causing the reaction to
    proceed more readily.

26
Functional Enzyme
  • Ribonuclease S (right) is an enzyme that breaks
    up RNA molecules.
  • The red areas designate the active site and
    comprise certain amino acid 'R' groups.
  • The substrate (in this case, RNA) is drawn into
    the active site, putting the substrate molecule
    under stress, thereby causing the reaction to
    proceed more readily.
  • Nearly all enzymes are made of protein, although
    RNA can also have enzymic properties.
  • Some enzymes contain only protein.
  • Others, called conjugated protein enzymes,
    require additional components to complete their
    catalytic properties.
  • These may be permanently attached parts called
    prosthetic groups, or temporarily attached
    non-protein coenzymes, which detach after a
    reaction and may then participate with another
    enzyme in other reactions.

27
Conjugated Protein Enzymes
Coenzyme required Contains the apoenzyme
(protein) plus a coenzyme (non-protein) e.g.
Dehydrogenases NAD
Prosthetic group required Contains the apoenzyme
(protein) plus a prosthetic group e.g.
Flavoprotein FAD
28
Mechanism of Enzyme Action
Steps in Enzyme Activity In the induced fit model
of enzyme function, the enzyme fits to its
substrate somewhat like a lock and key, with the
shape of the enzyme changing when the substrate
fits into the cleft of the active site.
  • The specificity of the substrate is determined by
    the complexity of the binding sites.
  • The wrong substrates will not fit into the active
    site.
  • Some enzymes have specificity to a bond type
    (e.g. lipases break up any chain length of lipid).

29
Enzymes are Catalysts
  • Catalysts are substances that increase the rate
    of chemical reactions. All catalysts speed up
    reactions by
  • Influencing the stability of bonds in the
    reactants.
  • Providing an alternative reaction pathway the
    binding of reactants and enzyme can weaken bonds
    in the reactants and allow the reaction to
    proceed more easily.
  • Enzymes are biologicalcatalysts they alter the
    chemical equilibrium between the reactant and
    the product.
  • When the substrate attains the required energy
    it is able to change into the product or
    products.

30
Enzymes are Catalysts
  • Catalysts provide an alternative pathway of
    lower activation energy.

31
Effects of pH on Enzymes
  • Like all proteins, enzymes are denatured (made
    non-functional) by extremes of pH
    (acid/alkaline).
  • Within these extremes most enzymes are still
    influenced by pH.
  • There is a particular pH for optimum activity for
    each enzyme. This is because the active sites of
    the enzyme can be disabled by the wrong pH.

32
Temperature and Enzyme Activity
  • Reactions occur faster at higher temperatures,
    but the rate of denaturation of enzymes also
    increases at higher temperatures.
  • High temperatures break the disulfide bonds
    important for the tertiary structure of the
    enzyme.
  • This destroys the active sites and therefore
    makes the enzyme non-functional.

33
Enzyme Concentration And Enzyme Activity
  • Assuming that the amount of substrate is not
    limiting, an increase in enzyme concentration
    causes an increase in the reaction rate.
  • Cells may increase the amount of enzyme present
    by increasing the rate of its synthesis to meet
    demand.

34
Substrate Concentration Effect on Enzyme Activity
  • Assuming that the amount of enzyme is constant
    and non-limiting, an increase in substrate
    concentration causes a diminishing increase in
    the reaction rate.
  • A maximum rate is obtained at a certain substrate
    concentration where all enzymes are occupied by
    substrate. The reaction rate cannot increase
    further.

35
Effect of Cofactors on Enzymes
  • Cofactors are substances that are essential to
    the catalytic activity of some enzymes.
  • Cofactors may alter the shape of enzymes slightly
    to make the active sites functional or to
    complete the reactive site.
  • Enzyme cofactors can be inorganic, e.g. metal
    ions and iron-sulfur clusters, or organic
    compounds, which are known as coenzymes.
  • Many vitamins are coenzymes. Vitamins are organic
    molecules not synthesized by the body, e.g.
    vitamin K, B1, B6, and folate.

36
Enzyme Inhibition
  • Enzyme inhibitors are substances that prevent the
    normal action of an enzyme and thereby slow the
    rate of enzyme controlled reactions.
  • Enzyme inhibitors may or may not act reversibly.
  • In reversible inhibition, the inhibitor is
    temporarily bound to the enzyme, thereby
    preventing its function.
  • Reversible inhibition is often a means by which
    enzyme activity is regulated in the functioning
    cell.
  • In irreversible inhibition, the inhibitor
    (poison) may bind permanently to the enzyme and
    cause it to be permanently deactivated.

37
Reversible Inhibition
  • Reversible inhibitors are used to control the
    activity of enzymes.
  • There is often an interaction between the
    substrate or end product and the enzyme
    controlling the reaction.
  • Buildup of the end product or a lack of substrate
    may deactivate the enzyme. This deactivation can
    occur via competitive or noncompetitive
    inhibition.
  • Competitive inhibitors compete with the substrate
    for the active site.
  • Noncompetitive inhibitors bind to the enzyme, but
    not at the active site. The substrate can bind
    but enzyme function is impaired.
  • Allosteric inhibitors are non competitive
    inhibitorsthat prevent the substrate from
    binding.

Model of elastase and its inhibitor
38
Competitive Inhibition
  • Competitive inhibitors compete with the substrate
    for the active site, thereby blocking it and
    preventing its attachment to the substrate.
  • The inhibition is reversible.
  • Example Malonate is a powerful inhibitor of
    cellular respiration because it is a competitive
    inhibitor of the enzyme succinate dehydrogenase
    in the Krebs cycle, which catalyzes the oxidation
    of succinate to fumarate.

39
Non-Competitive Inhibition
  • Non-competitive inhibitors bind to the enzyme,
    but not at the active site, and alter its shape.
    The substrate is still able to bind, but the
    reaction rate is slowed because the enzyme is
    less able to perform its function.
  • Allosteric enzyme inhibitors are non competitive
    inhibitors that induce a shape change that alters
    the active site and prevents the substrate from
    binding.
  • In this case, the enzyme ceases to function.

40
Irreversible Inhibition
  • Irreversible enzyme inhibitors are poisons that
    prevent enzyme function.
  • Heavy metals Certain heavy metals bind tightly
    and permanently to the active sites of enzymes,
    destroying their catalytic properties.
  • Example mercury (Hg), cadmium (Cd), lead (Pb),
    and arsenic (As).
  • They are generally non-competitive inhibitors,
    although an exception is mercury which
    deactivates the enzyme papain.
  • Heavy metals are retained in the body, and lost
    slowly.
  • Insecticides
  • These can prevent the breakdown of acetylcholine
    (ACh), a neurotransmitter in the nervous system.
  • They bind to the enzyme that normally breaks down
    the ACh, causing over stimulation of the nerves.

41
Energy in Cells
  • Every living cell needs a regular supply of
    energy to power chemical processes
  • Sources of energy are large complex molecules
    which make up food supply
  • Energy is released when the bonds holding atoms
    together are released, usually as heat
  • Energy is used to form adenosine-tri-phosphate
    (ATP) from adenosine-di-phosphate (ADP)
  • ADP
  • ATP
  • Photosynthesis captures light energy and stores
    is in food glucose
  • Respiration releases energy from glucose
  • Energy is stored at ATP until it is needed

42
Respiration
  • Respiration is a process which makes ATP using
    energy in organic molecules such as glucose
    glycolysis, Krebs cycle and oxidative
    phosphorylation (electron transport chain).
  • If glucose is placed in oxygen and set alight, it
    burns and releases a lot of heat energy as the
    glucose molecules combine with oxygen to form
    carbon dioxide and water and the energy from
    glucose is rapidly transferred to heat energy.
    This is an oxidation reaction.
  • In a living cell, a similar process takes place,
    but in a more controlled way. You will recognise
    the equation
  • Glucose oxygen ? energy carbon
    dioxide water
  • C6H12O6 O2 ? energy
    CO2 H2O
  • This actually happens in a series of reactions
    controlled by enzymes and the energy in glucose
    is released in small stages. A sequence of
    reactions (like in the process of respiration) is
    called a metabolic pathway.

43
Glycolysis glucose converted to pyruvate
  • Occurs in the cytoplasm of the cell
  • Glucose (a 6 carbon compound) is converted into
    two pyruvate (pyruvic acid) molecules (a 3 carbon
    compound)
  • Small amount of ATP (adenosine triphosphate) is
    made in this process (2 ATP)

44
Kreb Cycle pyruvate fed into cycle of reactions
  • Occurs in the matrix of the mitochondria
  • If oxygen is available, pyruvate (pyruvic acid)
    formed in glycolysis passes into a mitochondrion
    through the outer and inner membranes
  • Link step to convert the pyruvate into a
    different molecule which then undergoes a cycle
    of reactions
  • Carbon dioxide removed (called decarboxylation)
    and diffuses out of the mitochondrion, out of the
    cell and out of organism
  • 2 ATP molecules produced
  • Hydrogen ions (H ions) and electrons are also
    produced in Krebs cycle to be fed into the
    electron transport chain to make more ATP

45
Oxidative Phosphorylation (electron transport
chain) - electrons produced passed along an
electron transport chain to produce ATP
  • This happens in the inner membrane of the
    mitochondrion
  • ATP is made by the addition of inorganic
    phosphate Pi to ADP. This is called a
    phosphorylation reaction. In respiration, this
    process needs oxygen so it is known as oxidative
    phosphorylation. The enzyme ATP synthase makes
    the ATP from ADP Pi
  • H ions and electrons pass through a series of
    reactions and energy is released as ATP. At the
    end of this electron transport chain, oxygen is
    needed.
  • Oxygen at the end of the electron transport chain
    combines with electrons and hydrogen ions to form
    water.
  • A lot of ATP is made in this part of respiration
    (34ATP molecules)

46
Anaerobic Respiration
  • When oxygen is not available, only glycolysis can
    occur. Therefore, a small amount of ATP is made
    (2 ATP) along with pyruvate
  • Pyruvate will inhibit glycolysis so it is
    converted to something else.
  • SOLUTIONS to remove the pyruvate
  • ALCOHOLIC FERMENTATION LACTIC FERMENTATION
  • Used by fungi plants Used by animals
  • Yeast converts pyruvate to ethanol Pyruvate is
    converted to lactic acid
  • Glucose ? pyruvate ? ethanol CO2 2 ATP
    Glucose ? pyruvate ? lactic acid 2 ATP
  • If yeast is supplied with a supply of Lactic
    acid build up in muscles causes the pain in
  • carbohydrate, it will carry out
    glycolysis exhausted muscles. The lactic acid is
  • and alcoholic fermentation. transported in the
    blood to the liver and here
  • it is converted back to pyruvic acid and
    then
  • to glucose during recovery.
  • The ethanol is used to make alcoholic
    drinks.
  • In baking, the CO 2 is used to make bread, This
    requires oxygen, which is why you

47
Summary of Respiration
48
Photosynthesis
  • Inputs CO2, H2O, light
  • CO2 is absorbed from air as gas
  • Water absorbed from environment
  • Light red and green light most
    photosynthetically active
  • Outputs C6H12O6, O2
  • C6H12O6 glucose temporarily stored as starch in
    leaves to be used in respiration
  • O2 is essentially a waste product that diffuses
    out
  • 6CO2 6H2O ? C6H12O6 6O2
  • Occurs in all green plants
  • Requires sunlight so leaves broad, thin and flat
    but also prone to water loss
  • Water loss decreased by waterproof cuticle which
    is a waxy layer on leaf
  • Stomata present to allow CO2 in and stop water
    loss

49
Photosynthesis
  • Transfer of light energy into chemical potential
    energy
  • Occurs in the grana of chloroplasts
  • Relied on by all organisms
  • Occurs in 2 stages
  • The light phase
  • Dark phase/Light independent phase (Calvin cycle)
  • Chlorophyll plays vital role in trapping light
    energy

50
Light Phase
Carries Energy
Light Independent Phase
51
Chromosomes
  • A Light microscope view of a chromosomefrom the
    salivary glands of the fly Simulium.
  • Banding groups of genes stained light and dark.
  • Puffing areas of transcription (mRNA
    production).
  • B Scanning electron microscope (SEM) view of sex
    chromosomes in the condensed state during acell
    division. Individual chromatin fibers are
    visible.
  • The smaller chromosome is the Y while
    thelarger one is the X.
  • C Transmission electron microscope (TEM) view of
    chromosomes lined up at the equator of a cell
    during the process of cell division. These
    chromosomes are also in the condensed state.

52
Chromosome States
  • Interphase Chromosomes are single-armed
    structures during their unwound state during
    interphase.
  • Dividing cells Chromosomes are double-armed
    structures, having replicated their DNA to form
    two chromatids in preparation for cell division.

53
Chromosome Structure
  • Histone proteins organize the DNA into tightly
    coiled structures (visible chromosomes) during
    cell division.
  • Coiling into compact structures allows the
    chromatids to separate without tangling during
    cell division.

54
Chromosome Features
  • Chromosomes can be identified by noting
  • Banding patterns
  • Position of the centromere
  • Presence of satellites
  • Length of the chromatids
  • These features enable homologous pairs to be
    matched and therefore accurate karyotypes to be
    made.

55
Chromosomes Contain Genes
  • A single chromosome may contain hundreds of
    genes.
  • Below are the locations of some known genes on
    human chromosomes

56
Nucleotides
  • The building blocks of nucleic acids (DNA and
    RNA) comprise the following components
  • a sugar (ribose or deoxyribose)
  • a phosphate group
  • a base (four types for each of DNA and RNA)

57
Structure of Nucleotides
  • The chemical structure of nucleotides

Symbolic form
58
Nucleotide Bases
Purines Adenine
Double-ringed structures Adenine
Double-ringed structures Guanine
Always pair up with pyrimidines Guanine
  • The base component of nucleotides which comprise
    the genetic code

Pyrimidines Cytosine
Single-ringed structures Cytosine
Single-ringed structures Thymine
Always pair up with purines Thymine
Thymine
Uracil
59
DNA Structure
  • Phosphates link neighboring nucleotides together
    to form one half of a double-stranded DNA
    molecule

60
DNA Molecule
  • Purines join with pyrimidines in the DNA molecule
    by way of relatively weak hydrogen bonds with the
    bases forming cross-linkages.
  • This leads to the formation of a double-stranded
    molecule of two opposing chains of nucleotides
  • The symbolic diagram shows DNA as a flat
    structure.
  • The space-filling model shows how, in reality,
    the DNA molecule twists into a spiral structure

61
DNA Replication 1
  • DNA is replicated to produce an exact copy of a
    chromosome in preparation for cell division.
  • The first step requires that the coiled DNA is
    allowed to uncoil by creating a swivel point.

62
DNA Replication 2
  • New pieces of DNA are formed from free nucleotide
    units joined together by enzymes.
  • The free nucleotides (yellow) are matched up to
    complementary nucleotides in the original strand.

63
DNA Replication 3
  • The two new strands of DNA coil up into a helix.
  • Each of the two newly formed DNA strands will go
    into forming a chromatid

64
DNA Replication 4
  • Free nucleotides with their corresponding bases
    are matched up against the template strand
    following the base pairing rule

A pairs with T
T pairs with A
G pairs with C
C pairs with G
65
Control of DNA Replication
  • DNA replication is controlled by enzymes at key
    stages

3'
5'
66
The Leading Strand
  • Enzymes can build strandsonly in the 5 to 3
    direction
  • This means that only one strand, called the
    leading strand, can be synthesized as a
    continuous strand.

67
The Lagging Strand
  • The other complementary strand, called the
    lagging strand, must be constructed in fragments,
    which are later joined together

68
Enzyme Control of Replication 4
69
The Cell Cycle
  • The process of mitosis is only part of a
    continuous cell cycle where most of the cell's
    'lifetime' is spent carrying out its prescribed
    role a phase in the cycle called interphase.
  • Interphase is itself divided up into three
    stages
  • G1 First Gap
  • S Synthesis
  • G2 Second Gap
  • Mitosis is the process bywhich the cell
    producestwo new daughter cellsfrom the original
    parent cell

70
Mitosis
71
Mitosis Micrographs
  • Cell division for somatic growth and repair

72
Meiosis
  • The purpose of meiosis is to produce haploid sex
    cells.
  • Haploid sex cells have only one copy of each
    homologous pair of autosomes plus one sex
    chromosome

73
Meiosis I
  • The first division of meiosis is called a
    reduction division because it reduces (halves)
    the number of chromosomes.
  • One chromosome from each homologous pair is
    donated to each intermediate cell

74
Meiosis II
  • The second division of meiosis is called a
    mitotic division, because it is similar to
    mitosis.
  • Sister chomatids of each chromosome are pulled
    apart and are donated to each gamete cell

75
Meiosis Mitosis Compared
76
Prokaryotes
  • Single-celled bacteria and cyanobacteria
  • The chromatin materia (DNA) is not held in a
    membrane
  • The chromosome is a simple DNA chain with the
    ends joined to form a circle
  • The cells do not have membrane-bound organelles

77
Eukaryotes
  • Higher cells that have a true nucleus
  • The chromatin material (DNA) is enclosed within a
    nuclear membrane
  • The chromosome is a length of DNA folded like a
    concerta. It is wound around proteins called
    histones, with other proteins present
  • Cells have membrane bound organelles and form
    spindles during mitosis and meiosis
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