Protein PGHT

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    Protein: Amino Acids

    10/24/20111

    Protein and Amino Acids

    Protein: a compound composed of C, H, O and

    N atoms, arranged into amino acids linked in a

    chain.

    Amino acid: a building block of protein, a

    compound containing amino group and anacid group attached to a central carbon atom.

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    Structure of Amino Acids

    Central C is connected to three compounds:

    amino group (NH2), acid group (COOH), and

    hydrogen (H).

    Central C is also another atom or group of

    atoms that varies one amino acid to another.

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    Structure of Amino Acids

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    20 Amino Acids

    G Glycine Gly P Proline Pro

    A Alanine Ala V Valine Val

    L Leucine Leu I Isoleucine Ile

    M Methionine Met C Cysteine Cys

    F Phenylalanine Phe Y Tyrosine Tyr

    W Tryptophan Trp H Histidine HisK Lysine Lys R Arginine Arg

    Q Glutamine Gln N Asparagine Asn

    E Glutamic Acid Glu D Aspartic Acid Asp

    S Serine Ser T Threonine Thr

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    Aromatic Amino Acids

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    Amino Acid Sequence

    Dipeptide: two amino acids bonded together

    by peptide bond.

    Tripeptide: three amino acids bonded

    together by peptide bond.

    Polypeptide: many (ten or more) amino acids

    bonded together by peptide bond.

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    Amino Acid Sequence

    Oligopeptide: an intermediate string of

    between four to ten amino acids bonded by

    peptide bond.

    Peptide bond: a bond between amine group

    of one and carboxyl group of another aminoacid.

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    Amino Acid Sequence

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    Myosin Light Chain (pork)msfsadqiae fkeafllfdr tgeckitlsqvgdvlralgt nptnaevkkv lgnpsneemnakkiefeqfl pmlqaisnnk dqgsyedfveglrvfdkegn gtvmvtelrh vlatlgekmkeeevealmag qedsngciny eafvkhimsi

    1

    31

    61

    91

    121

    30

    60

    90

    120

    150

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    Structure of Protein

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    Structure of Protein

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    Protein Synthesis

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    Complete and Incomplete Proteins

    Complete proteins, meaning that all

    indispensable AAs are present.

    Incomplete proteins, meaning that one or

    more of the indispensable AAs was absent.

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    Dispensable and Indispensable Amino

    Acids

    Dispensable alanine

    glutamic acid

    aspartic acid

    Glycine

    serine

    proline

    glutamine(a)

    asparagine

    cysteine (b)

    tyrosine (b)

    Indispensable Lysine

    isoleucine (c)

    leucine (c)

    valine

    Histidine

    Threonine

    Methionine

    Phenylalanine

    tryptophan

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    Dispensable and Indispensable Amino

    Acids

    a. Conditionally indispensable under times of

    severe bodily stress

    b. Conditionally indispensable if methionine

    and phenylalanine are not available

    c. Leucine, isoleucine, and valine are called

    branch chain amino acids (BCAAs) because

    of their structure.

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    Complex proteins

    Lipoproteins contain lipid subunits in addition to the

    amino acid.

    Glycoproteins contain carbohydrate subunits.

    Phosphoproteins contain phosphoric acid, and

    nucleoproteins contain nucleic acids.

    Some proteins have important smaller molecules,

    known as prosthetic groups, attached to their

    surfaces.

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    Enzymes: A Function of Protein

    Protein catalysts

    Enzymes are protein molecules that regulate

    the metabolism of proteins, carbohydrates

    and fats.

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    Roles of Protein

    Fluid and acid-base balance,

    Antibodies and hormones,

    Nutrient transportation,

    Blood clotting,

    Muscle contraction,

    Blood vessel expansion,

    Contraction to maintain normal blood pressure,

    Connective tissues,

    Visual pigments

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    Biologically Active Peptides

    Peptides that are inactive in the sequence of

    the parent protein, but can be released duringenzymatic digestion or food processing, and

    have health benefits to the body.

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    Biologically Active Peptides

    Antihypertensive activity,

    Antibacterial activity,

    Mineral-binding activity,

    Enhancement of intestinal activity

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    Peptide Sequences Showing

    Antihypertensive Effect

    Milk protein (casein, sour milk, whey protein)

    Poultry (chicken muscle, ovalbumin)

    Several kinds of fish (sardine, bonito, salmon)

    Porcine skeletal muscle protein (actin, myosin,troponin)

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    Protein Quality

    Essential amino acid: an amino acid that the

    body cannot synthesize in amounts sufficientto meet physiological need.

    Non essential amino acid: an amino acid that

    can be synthesized in the body.

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    Protein Quality

    Complete protein: a protein containing all the

    essential amino acids in human nutrition in

    amounts of adequate for human use.

    High-quality protein: an easily digestible

    complete protein that amino acids fit theprotein needed by human body.

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    Protein Quality

    Limiting amino acid: the essential amino acid

    found in the shortest supply relative to the

    amounts needed for protein synthesis in the

    body.

    Digestibility: the measure of the amount of

    amino acids absorbed from protein intake.

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    Protein Digestibility

    Food source Protein digestibility (%)

    Egg 97

    Milk and cheese 97

    Mixed US diet 96

    Peanut butter 95

    Meat and fish 94

    Whole wheat 86

    Oatmeal 86

    Soybeans 78

    Rice 76

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    Protein Quality

    Reference protein: egg protein is used as a

    standard against which to measure the quality

    of other proteins.

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    Protein Quality

    Reference protein: egg protein is used as a

    standard against which to measure the quality

    of other proteins.

    Nitrogen balance: the amount of nitrogen

    consumed (N-in) as compared to the amount

    of nitrogen excreted (N-out).

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    Protein Quality

    The average amino acid weight is about 6.25

    times as much as the nitrogen it contains, sothe scientists can estimate the amount of

    protein in a sample of food, body tissue, or

    excrete by multiplying the weight of nitrogen

    in by 6.25.

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    Nitrogen Balance

    Nitrogen equilibrium/zero nitrogen balance:

    N-in = N-out

    Positive nitrogen balance: N-in > N-out

    Negative nitrogen balance: N-in < N-out

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    Measures of Protein Quality

    Chemical score: a rating of the quality of a test

    protein arrived at by comparing its amino acid

    pattern with that of a reference protein.

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    Reference Pattern for Chemical Score of

    Protein

    Essential amino acids Whole egg

    mg AA per g N

    Histidine 148

    Isoleucine 340

    Leucine 540

    Lysine 440

    Methionine 355

    Phenylalanine 580

    Threonine 294

    Tryptophan 106

    Valine 410

    Total 3,210

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    Measures of Protein Quality

    Biological value (BV): the amount of protein

    nitrogen that retained from a given amount of

    protein that has been digested and absorbed.

    BV = [Food N (Fecal N Metabolic N) (Urinary N

    Endogenous N)] / [Food N (Fecal N Metabolic N)]

    x 100

    BV = N retained / N absorbed x 100

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    Biological Value of Proteins

    Protein Biological Value

    Egg 100

    Milk 93

    Rice 86

    Beef, fish 75

    Corn 72

    Peanut flour 56

    Wheat gluten 44

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    Measures of Protein Quality

    Net protein utilization (NPU): the amount of

    protein nitrogen that is retained from a givenamount of protein nitrogen eaten.

    NPU = [Food N (Fecal N Metabolic N) (UrinaryN Endogenous N)] / Food N x 100

    NPU = N retained / N intake x 100

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    Measures of Protein Quality

    Protein efficiency ratio (PER): the weight

    gained from protein intake.

    PER = Weight gain (g) / Protein intake (g)

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    Protein-kCalorie Malnutrition

    Kwashiorkor: a malnutrition caused by protein

    deficiency in the presence of adequate

    kcalories.

    Marasmus: a malnutrition caused by

    inadequate kcalories.

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    Recommended Protein Intakes

    RDA = 0.8 g/kg body weight.

    Factors are considered in establishing

    recommended protein intake:

    Body weight

    Lean body

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    Protein Sources

    Animal foods

    Cereals

    Vegetables

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    Protein Digestion and Absorption

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    Digestion

    Process that breaks down food into molecules

    small enough to absorb.

    Break polymers into monomers that are easier

    to absorb and that can be used to synthesize

    new polymers required by the organism.

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    Absorption

    Cells that line tract take up nutrients

    Nutrients move to cells where they are

    Incorporated into the cells

    Converted to energy which may be used

    immediately or stored until needed

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    Di dalam Mulut

    Tidak terjadi digesti protein yang signifikan di dalam

    mulut, hanya membasahi jaringan konektif (protein

    kolagen).

    Distimulasi dengan timbulnya bau, indra penglihatan

    dan rasa, atau pemikiran mengenai makanan,

    menyebabkan saliva tersekresi.

    Saliva mengandung: mucin (a glycoprotein lubricant),

    amylase (untuk memecah KH dan glikogen)

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    Di dalam Lambung (Stomach)

    Distimulasi dengan aliran makanan, menyebabkan neurotransmitters acetylcholine

    dan histamine dihasilkan oleh sel-sel dalam lambung (stomach)

    Distimulasi dengan adanya makanan di dalam lambung, mengakibatkan hormone

    gastrin tersekresi.

    Kombinasi acetylcholine, histamine dan gastrin menyebabkan cairan lambung(gastric juices) tersekresi.

    mucin selalu disekresikan dalam stomach

    HCl - pH 0.8-2.5 (disekresikan parietal cells)

    pepsinogen (zymogen, disekresikan oleh chief cells)

    gastric lipase (enzyme yang meemecah lemak, tetapi aktif di intestine)

    Protein terdenaturasi akibat pH rendah

    Nilai pH yang rendah berfungsi sebagai antiseptik, dan membunuh bakteri dan sel

    asing.

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    Digesti dalam lambung

    Zymogen Pepsinogen (MW=40,000) yang dihasilkan

    di dalam lambung diaktivasi oleh adanya enzim

    pepsin dan asam lambung. Pepsinogen memiliki 42

    potongan asam amino untuk menjadi enzim pepsin

    (MW=33,000) dan fragmen peptida yang akan

    terdegradasi. Pepsin akan mendigesti secara parsial dengan

    memotong ikatan peptida pada ujung N asam amino

    aromatis (Phe, Tyr, Trp)

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    Digesti dalam Duodenum

    Cairan lambung yang disebut Chyme masuk ke duodenum, pH

    rendah memicu sekresi hormon secretin dalam darah. Asam amino

    menstimulasi sekresi cholecystokinin.

    Secretin menstimulasi pankreas untuk mensekresikan bicarbonat ke

    dalam usus kecil (small intestine), (pH changes to about 7).

    Cholecystokinin menstimulai sell exocrine pancreas untuk

    mensekresikan trypsinogen, chymotrypsinogen dan

    procarboxypeptidase ke dalam intestine. (Sel exocrine juga

    mengandung protein trypsin inhibitor untuk melindungi diri dari

    free trypsin).

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    Digesti dalam Duodenum

    Sel-sel intestinal mensekresikan enzim yang disebut enteropeptidase yangbertugas pemotongan trypsinogen menjadi trypsin.

    Trypsin merubah chymotrypsinogen menjadi chymotrypsin,procarboxypeptidase menjadi carboxypeptidase dan proelastase menjadielastase (belum diketahui asal-nya dari mana), dan trypsinogen menjaditrypsin.

    Trypsin memotong peptida pada ujung karboksil asam amino Lys dan Arg.

    Chymotrypsin memotong ujung karboksil asam amino aromatis Phe, Tyr

    dan Trp.

    Enzim yang membutuhkan Zn.

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    Digesti dalam Duodenum

    Carboxypeptidase memotong semua asam amino pada fragmen

    yang masih memiliki satu asam amino pada ujung karboksil (akan

    memotong pada sisi ujung N dari ujung C asam amino).

    Elastase memotong derivat asam amino, desmosine.

    Aminopeptidase merupakan sekresi sel usus halus dan bertugas

    memotong ujung N asam amino pada semua peptida.

    Banyak protein terdigesti secara sempurna menjadi asam amino,diserap dan kemudian diangkut ke dalam darah menuju sel-sel

    dalam tubuh.

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    Digesti dalam Duodenum

    Keratin dan protein fibrosa lainnya sulit untuk

    didigesti (hanya lewat).

    Kebanyakan protein tanaman tertutup

    selulosa dan tidak dapat didigesti.

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    Component of Gastrointestinal

    System

    Mouth

    Oral cavity

    Tongue

    Pharynx

    Salivary Glands

    Esophagus

    Stomach

    Liver

    Gall Bladder

    Pancreas

    Small Intestine

    Large Intestine

    Rectum

    Anus

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    Oral Cavity

    Food enters the mouth and is reduced in size

    by teeth and tongue.

    Salivary glands secrete saliva which

    Lubricates

    Buffers

    Contains antimicrobial substances

    Contains amylase to digest starch

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    http://www.vh.org/Providers/Textbooks/motilitygastro/7.htmlhttp://arbl.cvmbs.colostate.edu/hbooks/pathphys/digestion/pregastric/salivary.htmlhttp://arbl.cvmbs.colostate.edu/hbooks/pathphys/digestion/pregastric/salivary.htmlhttp://arbl.cvmbs.colostate.edu/hbooks/pathphys/digestion/pregastric/esophagus.htmlhttp://www.ee.ualberta.ca/~mintchev/stomach.htmlhttp://www.vh.org/Providers/Textbooks/LiverPathology/Text/AtlasLiverPathology.htmlhttp://www.cag-acg.org/patinfo/gall_bladder.htmhttp://www.fda.gov/fdac/features/896_panc.htmlhttp://arbl.cvmbs.colostate.edu/hbooks/pathphys/digestion/smallgut/index.htmlhttp://arbl.cvmbs.colostate.edu/hbooks/pathphys/digestion/largegut/index.htmlhttp://arbl.cvmbs.colostate.edu/hbooks/pathphys/digestion/largegut/index.htmlhttp://arbl.cvmbs.colostate.edu/hbooks/pathphys/digestion/smallgut/index.htmlhttp://www.fda.gov/fdac/features/896_panc.htmlhttp://www.cag-acg.org/patinfo/gall_bladder.htmhttp://www.vh.org/Providers/Textbooks/LiverPathology/Text/AtlasLiverPathology.htmlhttp://www.ee.ualberta.ca/~mintchev/stomach.htmlhttp://arbl.cvmbs.colostate.edu/hbooks/pathphys/digestion/pregastric/esophagus.htmlhttp://arbl.cvmbs.colostate.edu/hbooks/pathphys/digestion/pregastric/salivary.htmlhttp://www.vh.org/Providers/Textbooks/motilitygastro/7.html
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    Swallowing

    Food passes to pharynx which contains both

    trachea and esophagus

    Epiglottis prevents food from entering trachea

    Food passes through esophagus into the

    stomach

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    Stomach

    Stores and digests food

    Contains pits leading to Gastric glands with

    three types of cells:

    Mucous cells - produce mucous which lubricates

    and protects lining. Parietal cells - secrete hydrochloric acid

    Chief cells - secrete pepsinogen

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    Small Intestine

    Receives food from stomach

    Bile from liver via the Gall bladder (kantung

    empedu)

    Enzymes from pancreas

    Site of most digestion

    Site of most absorption

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    Duodenum

    First 25 cm of small intestine

    Receives enzymes from pancreas

    Neutralizes acid from stomach

    Site of most chemical changes in food

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    Enzymes

    Fat + bile and lipase = Fatty acids + glycerol

    Starch + Amylase = simple sugars

    Maltose + maltase = glucose + glucose

    Sucrose + sucrase = glucose + fructose

    Lactose + lactase = glucose + galactose

    Protein + protease = amino acids

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    Pancreas

    Releases critical enzymes for digestion

    Neutralize acid by releasing bicarbonate

    Insufficient pancreatic function can lead to

    starvation

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    Liver

    Produces bile

    No digestive enzymes, but contains bile salts

    Emulsifies fats

    Made from cholesterol

    Stored in Gall Bladder

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    Enzymatic Action - Carbohydrates

    Starch broken down into the disaccharide , maltose, by

    pancreatic amylases.

    Disaccharides converted to monosaccharides

    Maltose is hydrolyzed by Maltase to give Glucose + Glucose

    Sucrose is hydrolyzed by Sucrase to give Glucose + Fructose

    Lactose is hydrolyzed by Lactase to give Glucose + Galactose

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    Absorption

    Following enzymatic action in the duodenum,

    food is absorbed in the remainder of the small

    intestine

    Has a very large surface area

    Contains Villi and microvilli

    Rich in capillaries and lymph vessels

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    http://orion1.paisley.ac.uk/courses/stfunmac/glossary/bile.html
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    Large Intestine

    Material not be digested or absorbed passes

    into the large intestine.

    90% of the water is absorbed into blood

    Some vitamins are produced by bacteria and

    are absorbed

    Residue is stored in rectum

    Eliminated through the anus

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    How are proteins absorbed?

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    How are proteins absorbed?

    The absorptive cells of the small intestine can only

    absorb individual amino acids, dipeptides ortripeptides.

    Once transported inside the cells all di/tripeptides are

    broken down into individual amino acids by proteases

    within the cells.

    Like monosaccharides, the amino acids are transported

    out of the absorptive cells and diffuse into the

    capillaries to move into general circulation.

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    THANK YOU

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