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Aulani "Biokimia" Presentation 5 Protein: Amino Acids Aulanni’am Biochemistry Laboratory Chemistry Departement Brawijaya University.

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Presentation on theme: "Aulani "Biokimia" Presentation 5 Protein: Amino Acids Aulanni’am Biochemistry Laboratory Chemistry Departement Brawijaya University."— Presentation transcript:

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2 Aulani "Biokimia" Presentation 5 Protein: Amino Acids Aulanni’am Biochemistry Laboratory Chemistry Departement Brawijaya University

3 Aulani "Biokimia" Presentation 5 Proteins have an amino group, an acid, a hydrogen, carbon molecule and a carbon side chain. Proteins have an amino group, an acid, a hydrogen, carbon molecule and a carbon side chain. Protein means primary or first and are necessary for life. Protein means primary or first and are necessary for life. Amino means contains nitrogen (NH 2). Amino means contains nitrogen (NH 2). Proteins can also contain sulfur, phosphorus or iron. Proteins can also contain sulfur, phosphorus or iron.

4 Aulani "Biokimia" Presentation 5 Amino Acids

5 Aulani "Biokimia" Presentation 5 COO - R group Amino group Carboxylic group L-Form Amino Acid Structure  H = Glycine CH 3 = Alanine H N 3 + H

6 Aulani "Biokimia" Presentation 5 HighLow Proton : abundant and small, affects the charge of a molecule H+H+ lone pair electrons H H H+H+ N H H N Amino H+H+ Ampholyte Ampholyte contains both positive and negative groups on its molecule Carboxylic C O O H C O O pKapKa LowHigh pKapKa

7 Aulani "Biokimia" Presentation 5 COOH NH 2 H + COO - R - C - HR - C - H NH 2 H + R - C - HR - C - H COO - NH 2 R - C - HR - C - H Acidic environment Neutral environment Alkaline environment +1 0 pK 1 ~ 2 pK 2 ~ 9 Isoelectric point 5.5

8 Aulani "Biokimia" Presentation [OH] → ★ ★ pK1pK1 pK2pK2 pH pI H-C-RH-C-R COO - NH 2 H + Isoelectric point = pK 1 + pK 2 2 Amino Acids Have Buffering Effect

9 Aulani "Biokimia" Presentation 5 Environment pH vs Protein Charge + Net Charge of a Protein Buffer pH Isoelectric point, pI

10 Aulani "Biokimia" Presentation 5 pKa = 1.8~2.4 pKa = 3.9~4.3 pKa = 6.0 pKa = 8.3 pKa = 10 pKa = 8.8~11 pKa = 10~ H+H+ + H+H+ + H+H+ + H+H+ + H+H+ + H+H+ + H+H+ -COOH-COO - aa -COOH-COO - RR -Imidazole·H + -Imidazole His -SH-S - Cys -OH-O - Tyr -NH 3 + -NH 2 aa -NH 3 + -NH 2 RR Smaller pKa releases proton easier Residues on amino acids can release or accept protons pKa of Amino Acid Residues Only His has the residue with a neutral pKa (imidazole) pKa of  carboxylic or amino groups is lower than pKa of the R residues

11 Aulani "Biokimia" Presentation 5 Amino acids -COOH-NH 2 -R GlyG AlaA ValV LeuL IleI SerS ThrT MetM PheF TrpW AsnN GlnQ ProP AspD GluE HisH CysC TyrY LysK ArgR pK1pK1 pK1pK1 pK2pK2 pK2pK2 pK3pK3 [OH - ] pH pI pI ? pK 1 + pK 2 2 three pKa two pKa ? ? p K a of Amino Acids

12 Aulani "Biokimia" Presentation 5 HOOC-CH 2 -C-COOH NH3+NH3+ H HOOC-CH 2 -C-COO - NH3+NH3+ H - OOC-CH 2 -C-COO - NH3+NH3+ H NH 2 H pK 1 = 2.1 pK 2 = 3.9 pK 3 = = 3.0 first second third Isoelectric point Isoelectric point is the average of the two pKa flanking the zero net-charged form pK1pK1 pK2pK2 pK3pK3 Aspartic acid [OH]

13 Aulani "Biokimia" Presentation 5 Amino Acids Nonessential amino acids Nonessential amino acids a.k.a dispensable amino acids can be made within the body a.k.a dispensable amino acids can be made within the body Essential amino acids Essential amino acids a.k.a indispensable amino acids must be obtained from foods a.k.a indispensable amino acids must be obtained from foods Conditionally essential amino acids are needed from food sources if the building blocks to make them are not available. Conditionally essential amino acids are needed from food sources if the building blocks to make them are not available.

14 Aulani "Biokimia" Presentation 5 An Essential Amino Acid

15 Aulani "Biokimia" Presentation 5 Nonessential Amino Acids

16 Aulani "Biokimia" Presentation 5 Most amino acids are neutral with an aliphathic (single chain) or aromatic chain. Most amino acids are neutral with an aliphathic (single chain) or aromatic chain. Two are dibasic with two amino groups: Two are dibasic with two amino groups: Histidine and arginine Histidine and arginine A few are diacidic and are commonly used as components of proteins in cell membranes A few are diacidic and are commonly used as components of proteins in cell membranes

17 Aulani "Biokimia" Presentation 5 Proteins Peptide bonds connect the acid end of one amino acid with the amino end of another. Peptide bonds connect the acid end of one amino acid with the amino end of another. They are the links that form a protein chain, which can be simple or very complex. They are the links that form a protein chain, which can be simple or very complex.

18 Aulani "Biokimia" Presentation 5 Dipeptide

19 Aulani "Biokimia" Presentation 5 NH 2 COOH 1 NH2NH2 2 NH 2 C NCOOH O H 21 Amino acids are connected head to tail Formation of Peptide Bonds by Dehydration Dehydration -H 2 O Carbodiimide

20 Aulani "Biokimia" Presentation 5 A Tripeptide consists of three amino acids linked together. A Tripeptide consists of three amino acids linked together. When there are three or more amino acids, the protein starts to form three dimensional shapes. When there are three or more amino acids, the protein starts to form three dimensional shapes.

21 Aulani "Biokimia" Presentation 5 Protein structure Remember Starch?: Remember Starch?: glucose+glucose+glucose+glucose+glucose… glucose+glucose+glucose+glucose+glucose… Meet Protein: Meet Protein: amino acid+amino acid+amino acid+amino acid… amino acid+amino acid+amino acid+amino acid… Made of 20 different amino acids bonded together in different sequences to form many SPECIFIC proteins. Made of 20 different amino acids bonded together in different sequences to form many SPECIFIC proteins.

22 Aulani "Biokimia" Presentation 5 Amino acids Essential (10) Essential (10) Phenylalanine Phenylalanine Valine Valine Threonine Threonine Tryptophan Tryptophan Isoleucine Isoleucine Methionine Methionine Histidine Histidine Arginine Arginine Leucine Leucine Lysine Lysine Conditionally essential (3) Conditionally essential (3) Cysteine Cysteine Glutamine Glutamine Tyrosine Tyrosine Nonessential (10) Alanine Asparagine Aspartic acid Cysteine Glutaminc acid Gluatmine Glycine Proline Serine Tyrosine

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24 Elemental composition of protein Element% Carbon Hydrogen Nitrogen Oxygen Sulfur Phosphorous 51.0 – – – – – – 1.5

25 Aulani "Biokimia" Presentation 5 Classification of amino acids Essential amino acid Essential amino acid One that the body is unable to make or can only make in inadequate quantities One that the body is unable to make or can only make in inadequate quantities Need to be consumed from the diet Need to be consumed from the diet 8-10 essential amino acids 8-10 essential amino acids Nonessential amino acid Nonessential amino acid One that the body can make in large enough quantities One that the body can make in large enough quantities Made from essential amino acids Made from essential amino acids Not necessary to consume these in the diet Not necessary to consume these in the diet nonessential amino acids nonessential amino acids

26 Aulani "Biokimia" Presentation 5 Classification, cont. Conditionally essential amino acid. One that can become essential in certain physiologic conditions 3 of these Example: Tyrosine becomes essential in people with “Phenylketonuria (PKU)”

27 Aulani "Biokimia" Presentation 5 Structure levels in proteins primary structure secondary structure tertiary structure quatery structure amino acid sequence spatial arrangement of amino acids within a poly- peptide chain (  helix, ß-sheet, unstructured turns) spatial arrangement of secondary structural elements subunit interactions

28 Aulani "Biokimia" Presentation 5 Amino acids are constituents of proteins there are about 20 proteinogenic amino acids

29 Aulani "Biokimia" Presentation 5 Structure of amino acids Different side chains make different amino acids C H C OH O Central carbon NH H H Acid group Amino group Side chain (R)

30 Aulani "Biokimia" Presentation 5 Likage of amino acids

31 Aulani "Biokimia" Presentation 5 Primary structure of a protein It is the sequence of amino acids that makes each protein different from the next It is the sequence of amino acids that makes each protein different from the next Dipeptide = 2 amino acids Dipeptide = 2 amino acids Tripeptide = 3 amino acids Tripeptide = 3 amino acids Polypeptide = many amino acids Polypeptide = many amino acids Most proteins have many 100 amino acids Most proteins have many 100 amino acids Peptide Bonds It is the sequence of amino acids that makes each protein different from the next It is the sequence of amino acids that makes each protein different from the next Dipeptide = 2 amino acids Dipeptide = 2 amino acids Tripeptide = 3 amino acids Tripeptide = 3 amino acids Polypeptide = many amino acids Polypeptide = many amino acids Most proteins have many 100 amino acids Most proteins have many 100 amino acids Primary structure of a protein It is the sequence of amino acids that makes each protein different from the next It is the sequence of amino acids that makes each protein different from the next Dipeptide = 2 amino acids Dipeptide = 2 amino acids Tripeptide = 3 amino acids Tripeptide = 3 amino acids Polypeptide = many amino acids Polypeptide = many amino acids Most proteins have many 100 amino acids Most proteins have many 100 amino acids It is the sequence of amino acids that makes each protein different from the next It is the sequence of amino acids that makes each protein different from the next Dipeptide = 2 amino acids Dipeptide = 2 amino acids Tripeptide = 3 amino acids Tripeptide = 3 amino acids Polypeptide = many amino acids Polypeptide = many amino acids Most proteins have many 100 amino acids Most proteins have many 100 amino acids

32 Aulani "Biokimia" Presentation 5 Secondary structures  -helix ß-sheet

33 Aulani "Biokimia" Presentation 5 Secondary structure Alignment of polypeptides as a right-hand alpha helix Alignment of polypeptides as a right-hand alpha helix Stabilized by hydrogen bonds between carboxyl (C=O) and imido (NH) groups Stabilized by hydrogen bonds between carboxyl (C=O) and imido (NH) groups

34 Aulani "Biokimia" Presentation 5 Unstructured turns connect secondary structural elements limited turnpronounced turn

35 Aulani "Biokimia" Presentation 5 Tertiary structure helices are shown in yellow, carbon backbone is shown in black

36 Aulani "Biokimia" Presentation 5 Tertiary structure Three dimensional folding and coiling of polypeptide into globular 3-D structure Three dimensional folding and coiling of polypeptide into globular 3-D structure Caused by additional chemical interactions among side chains Caused by additional chemical interactions among side chains Disulfide bonds Disulfide bonds

37 Aulani "Biokimia" Presentation 5 Quaternary structure Interactive folding of several polypeptide chains together to form a “single” functional protein Interactive folding of several polypeptide chains together to form a “single” functional protein Functional proteins also might incorporate minerals or other nonprotein components Functional proteins also might incorporate minerals or other nonprotein components Final shape and components determine function of protein Final shape and components determine function of protein

38 Aulani "Biokimia" Presentation 5 Quartery structure T-form compact structure R-form relaxed structure

39 Aulani "Biokimia" Presentation 5 Polypeptide Polypeptide Copyright 2005 Wadsworth Group, a division of Thomson Learning

40 Aulani "Biokimia" Presentation 5 Proteins Amino acid sequences can vary resulting in almost an endless number of combinations. Amino acid sequences can vary resulting in almost an endless number of combinations. Each protein’s sequence is determined by the DNA Each protein’s sequence is determined by the DNA As each amino acid has unique chemical characteristics and electrical charges, the resulting shapes can be very complex. As each amino acid has unique chemical characteristics and electrical charges, the resulting shapes can be very complex.

41 Aulani "Biokimia" Presentation 5 Protein shape and function

42 Aulani "Biokimia" Presentation 5 Enzymes Proteins that catalyze (speed up) chemical reactions without being used up or destroyed in the process. Proteins that catalyze (speed up) chemical reactions without being used up or destroyed in the process. Anabolic (putting things together) and catabolic (breaking things down) functions. Anabolic (putting things together) and catabolic (breaking things down) functions. Examples Examples Digestion Digestion Salivary amylase Salivary amylase Trypsin Trypsin

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45 Hormones Chemical messengers that are made in one part of the body but act on cells in other parts of the body. Chemical messengers that are made in one part of the body but act on cells in other parts of the body. Note that "steroid hormones" are not proteins! Note that "steroid hormones" are not proteins! Examples Examples Insulin Insulin CCK CCK Some reproductive hormones Some reproductive hormones

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47 Immune function (antibodies) Antibodies are proteins that attack and inactivate bacteria and viruses that cause infection. Antibodies are proteins that attack and inactivate bacteria and viruses that cause infection.

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49 Denaturation Protein denaturation happens when a protein changes its shape, usually uncoiling. This changes its function and properties. An egg is mostly liquid until cooked. Milk becomes yogurt or or cheese when acids or enzymes are added.. Heat, acids, bases, alcohol, heavy metals, enzymes or other agents can cause denaturation.

50 Aulani "Biokimia" Presentation 5 Protein Digestion Stomach releases HCL, which denatures (uncoils) protein strands and converts the inactive form of pepsinogen into the active form pepsin. Stomach releases HCL, which denatures (uncoils) protein strands and converts the inactive form of pepsinogen into the active form pepsin. Pepsin breaks the proteins into smaller polypeptides Pepsin breaks the proteins into smaller polypeptides Pepsin is one of thousands of enzymes, which allows chemical reactions to take place in the body without being affected itself. Pepsin is one of thousands of enzymes, which allows chemical reactions to take place in the body without being affected itself.

51 Aulani "Biokimia" Presentation 5 Small Intestine Releases pancreatic and intestinal proteases. Releases pancreatic and intestinal proteases. These hydolyze the polypeptides further into tripeptides, dipeptides and finally amino acids, which are actively transported into SI cells and then released into the blood stream. These hydolyze the polypeptides further into tripeptides, dipeptides and finally amino acids, which are actively transported into SI cells and then released into the blood stream.

52 Aulani "Biokimia" Presentation 5 Protein Digestion in the GI Tract

53 Aulani "Biokimia" Presentation 5 Protein Absorption Carriers - cells of the villi of the SI have gates through which carrier substances transport the amino acids. Carriers - cells of the villi of the SI have gates through which carrier substances transport the amino acids. Capillaries, which are the smallest branches of the circulatory system carry the free amino acids from the villi throughout the body. Capillaries, which are the smallest branches of the circulatory system carry the free amino acids from the villi throughout the body. Absorption misconceptions Absorption misconceptions Enzyme/amino acid supplements Enzyme/amino acid supplements

54 Aulani "Biokimia" Presentation 5 Messenger RNA from the nucleus and Ribosomes within cells assemble the free amino acids into proteins As the ribosome moves along the mRNA, an enzyme bonds one amino acid to another. 40 to 100 amino acids can be added to a growing protein strand in one second.

55 Aulani "Biokimia" Presentation 5 Protein Synthesis DNA in the cell nucleus gives mRNA the instructions. DNA in the cell nucleus gives mRNA the instructions. mRNA goes into the cellular fluid and attaches itself to ribosomes mRNA goes into the cellular fluid and attaches itself to ribosomes transfer RNA carries free amino acids to the mRNA transfer RNA carries free amino acids to the mRNA Ribosomes move along the mRNA allowing enzymes to bond one amino acid to another until the completed protein is finished and released. Ribosomes move along the mRNA allowing enzymes to bond one amino acid to another until the completed protein is finished and released.

56 Aulani "Biokimia" Presentation 5 Protein Synthesis

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59 Sequencing errors

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61 When a cell makes a protein it is said that that gene is expressed. Nearly all the body’s cells can make all human proteins, but each type of cell makes only the kinds of proteins it needs.

62 Aulani "Biokimia" Presentation 5 Roles of Proteins Building material Growth, a matrix of protein underlies almost all structures in the body including bones,muscles ligaments, tendons, connecting matrix between cell walls, scar tissue, hair and nails. Maintenance, GI tract cells are replaced every three days. The whole body has its cells renewed every seven years.

63 Aulani "Biokimia" Presentation 5 Proteins as Enzymes Proteins as Enzymes Enzymes are usually composed of a protein, a vitamin and a trace mineral. They act as catalysts, allowing reactions to occur more quickly and efficiently. They can cause two substances to come together making a new structure or can split a compound apart. An enzyme is not affected by the chemical reactions it allows to take place.

64 Aulani "Biokimia" Presentation 5 Roles of Proteins Enzymes Enzymes

65 Aulani "Biokimia" Presentation 5 Hormones Hormones

66 Aulani "Biokimia" Presentation 5 Roles of Proteins Regulation of fluid balance Regulation of fluid balance Dependent edema may be caused when there is too much fluid between cells and not enough hydrophilic protein within the cells. Dependent edema may be caused when there is too much fluid between cells and not enough hydrophilic protein within the cells. Acid-base regulation, proteins act as buffers accepting and releasing hydrogen ions thus preventing acidosis or alkalosis. Acid-base regulation, proteins act as buffers accepting and releasing hydrogen ions thus preventing acidosis or alkalosis.

67 Aulani "Biokimia" Presentation 5 Transport Proteins

68 Aulani "Biokimia" Presentation 5 Proteins in Immunity Antibodies are giant proteins that bind up specific invaders like viruses or antigens Antibodies are giant proteins that bind up specific invaders like viruses or antigens Antigens are substances that cause the body to produce antibodies. They may include bacteria, allergens, toxins or anything that causes an inflammatory response. Antigens are substances that cause the body to produce antibodies. They may include bacteria, allergens, toxins or anything that causes an inflammatory response.

69 Aulani "Biokimia" Presentation 5 Roles of Proteins Source of energy. The brain and nervous system must have glucose. Once the amino group is removed from the protein, the remaining carbon molecules can be used to create energy - 4 Kcal per gram or stored as fat. Source of energy. The brain and nervous system must have glucose. Once the amino group is removed from the protein, the remaining carbon molecules can be used to create energy - 4 Kcal per gram or stored as fat. Other roles include being converted to other proteins or making neurotransmitters norepinephrine and epinephrine, melanin, fibrin and as precursor to the vitamin niacin. Other roles include being converted to other proteins or making neurotransmitters norepinephrine and epinephrine, melanin, fibrin and as precursor to the vitamin niacin.

70 Aulani "Biokimia" Presentation 5 Roles of Proteins Other roles include being converted to other proteins or making: Other roles include being converted to other proteins or making: neurotransmitters norepinephrine and epinephrine neurotransmitters norepinephrine and epinephrine melanin melanin fibrin fibrin precursor to the vitamin niacin. precursor to the vitamin niacin.

71 Aulani "Biokimia" Presentation 5 Protein Metabolism Protein turnover Protein turnover Amino acid pool includes free amino acids from endogenous or exogenous sources Amino acid pool includes free amino acids from endogenous or exogenous sources Nitrogen balance Nitrogen balance Positive nitrogen balance during growth or when building new tissue Positive nitrogen balance during growth or when building new tissue Negative nitrogen balance if burned, fever, injury, infection or starvation. Negative nitrogen balance if burned, fever, injury, infection or starvation.

72 Aulani "Biokimia" Presentation 5 Protein Metabolism Using amino acids to make proteins. Using amino acids to make proteins. – Cells can dismantle one amino acid and combine the amino group of that amino acid with carbon fragments from glucose metabolism to make another essential or nonessential amino acid needed.

73 Aulani "Biokimia" Presentation 5 Protein Metabolism Deamination is the removal of the nitrogen containing amino group, converting it to ammonia, which is sent to the liver and converted into urea. The remaining carbon fragment may be burned or stored as fat. Amino acids can be used to make fat by removing the amino group and converting the remaining carbon fragments to fat.

74 Aulani "Biokimia" Presentation 5 Amino Acid Pool Proteins are degraded and resynthesized continuously Proteins are degraded and resynthesized continuously Several times more protein is turned over daily within the body (endogenous) than is consumed (exogenous) Several times more protein is turned over daily within the body (endogenous) than is consumed (exogenous) AA consumed in excess or unable to be used are not stored. They are: AA consumed in excess or unable to be used are not stored. They are: degraded into urea, uric acid, and creatinine degraded into urea, uric acid, and creatinine lost in feces or sweat lost in feces or sweat converted into hair and nails converted into hair and nails

75 Aulani "Biokimia" Presentation 5 Protein Quality High-quality proteins High-quality proteins Digestibility Digestibility Animal vs. plant Animal vs. plant Amino acid composition Amino acid composition Limiting amino acid Limiting amino acid

76 Aulani "Biokimia" Presentation 5 Protein Quality Is reflected in the amino acid score: content of individual essential AA in food Is reflected in the amino acid score: content of individual essential AA in food ÷ content of same AA in reference pattern Based on reference pattern for age Based on reference pattern for age Four AA are likely to be limiting Four AA are likely to be limiting Lysine, sulfur containing (methionine plus cystine), threonine and tryptophan Lysine, sulfur containing (methionine plus cystine), threonine and tryptophan

77 Aulani "Biokimia" Presentation 5 Protein Quality Reference protein Reference protein Complementary proteins Complementary proteins

78 Aulani "Biokimia" Presentation 5 Reference Proteins Nitrogen balance studies within age groups Nitrogen balance studies within age groups Used data for highy digestible, high quality proteins - egg, meat, milk or fish Used data for highy digestible, high quality proteins - egg, meat, milk or fish Amino acid scoring patterns were factored in Amino acid scoring patterns were factored in A margin of safety of 2 standard deviations to meet needs of 97.5% of the population A margin of safety of 2 standard deviations to meet needs of 97.5% of the population For adults over age 19 the reference protein intake is 0.75 g/kg/day (RDA is 0.8) For adults over age 19 the reference protein intake is 0.75 g/kg/day (RDA is 0.8) Range was egg to vegetable based diet Range was egg to vegetable based diet

79 Aulani "Biokimia" Presentation 5 Protein Quality Protein Digestibility Corrected AA Score compares the amino acid content of a protein with the human amino acid requirements and corrects for digestibility. Protein Digestibility Corrected AA Score compares the amino acid content of a protein with the human amino acid requirements and corrects for digestibility. Considers factors that limit digestion: Considers factors that limit digestion: cell walls, enzyme inhibitors, tannins cell walls, enzyme inhibitors, tannins Reveals the most limiting AA Reveals the most limiting AA

80 Aulani "Biokimia" Presentation 5 Protein Quality PDCAAS PDCAAS Protein digestibility-corrected amino acid score Protein digestibility-corrected amino acid score

81 Aulani "Biokimia" Presentation 5 Food Labels Quantity of protein Quantity of protein Daily Value Daily Value 50 g protein 50 g protein 10% of a 2000 kcal diet 10% of a 2000 kcal diet

82 Aulani "Biokimia" Presentation 5 Protein-Energy Malnutrition (PEM) Acute PEM when one is recently deprived of food. Children are thin for their height. Acute PEM when one is recently deprived of food. Children are thin for their height. Chronic PEM from long term food deprivation. Children are short for their age. Chronic PEM from long term food deprivation. Children are short for their age.

83 Aulani "Biokimia" Presentation 5 Protein-Energy Malnutrition Marasmus - inadequate energy and protein over a long period of time. Often seen at 6-18 months of age. Look like little old people. Marasmus - inadequate energy and protein over a long period of time. Often seen at 6-18 months of age. Look like little old people. Kwashiorkor - “the evil spirit that infects the first child when the second child is born.” Sudden deprivation at 18 mon to 2 yrs. Kwashiorkor - “the evil spirit that infects the first child when the second child is born.” Sudden deprivation at 18 mon to 2 yrs. Marasmus-kwashiorkor mix: edema of marasmus with wasting of kwashiorkor Marasmus-kwashiorkor mix: edema of marasmus with wasting of kwashiorkor

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86 Protein-Energy Malnutrition Infections: Antibodies needed to fight infections are degraded to provide amino acids for survival. Dysentery with concomitant diarrhea robs the body of needed nutrients. Rehabilitation: electrolytes especially potassium and sodium are given slowly over the first 2 days, then foods may be started in small quantities.

87 Aulani "Biokimia" Presentation 5 Health Effects of High Protein Heart disease: diet high in animal protein may contribute to a higher incidence of heart disease in the U.S. High homocysteine level possibly from suboptimal B 12, B 6 and/or folic acid is associated with heart disease. Cancer of the colon, breast, kidneys, pancreas and prostate is associated with high animal protein and fat diet. Adult bone loss. Calcium excretion rises as protein intake increases.

88 Aulani "Biokimia" Presentation 5 Health Effects of High Protein Diet Weight control helpful for some not all Any diet in which grains are severely limited should supplement with manganese 5 mg/day and selenium 200 ug Kidney disease - a high protein diet increases the load on the kidneys, which in Chinese medicine means degenerative changes will take place earlier. We are as old as our back is flexible and our kidneys function adequately.

89 Aulani "Biokimia" Presentation 5 Recommended Intakes RDA RDA g/kg/day for healthy adults 8-11% - of energy intake per day grams of protein per day or between 200 to 250 Kcal. protein. If junk food, sugar and fat is restricted, it is difficult not to get enough protein.

90 Aulani "Biokimia" Presentation 5 Recommended Intakes Calculate own: wt (lbs) divided by 2.2 x.8 Calculate own: wt (lbs) divided by 2.2 x.8 Adequate intake - if total Calories are too low, protein will be used to meet Calorie needs Adequate intake - if total Calories are too low, protein will be used to meet Calorie needs Protein in abundance Protein in abundance

91 Aulani "Biokimia" Presentation 5 Supplements Protein supplements- very active athletes may benefit from an intake of 1 gm of protein per kg rather than.8 gm/kg of body wt. (75 gm instead of 63 gm/day - 1 1/2 oz more meat) Amino acid supplements if not balanced may lead to deficiencies of some AA thru competition with carrier enzymes Lysine up to 3 gm a day may suppress herpes infection (divided doses with meals)

92 Aulani "Biokimia" Presentation 5 Vegetarian Diets Healthy food choices Healthy food choices Macrobiotic diets use too much salt and can be overly restrictive. However, they contribute one excellent idea - to eat as much as possible a variety of minimally processed, organic, locally grown foods in the season in which they are grown. Macrobiotic diets use too much salt and can be overly restrictive. However, they contribute one excellent idea - to eat as much as possible a variety of minimally processed, organic, locally grown foods in the season in which they are grown.

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