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Human Biochemistry B.5-9. nutrients Food required in the diet Food required in the diet Recommended daily intake Recommended daily intake Micro less than.

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Presentation on theme: "Human Biochemistry B.5-9. nutrients Food required in the diet Food required in the diet Recommended daily intake Recommended daily intake Micro less than."— Presentation transcript:

1 Human Biochemistry B.5-9

2 nutrients Food required in the diet Food required in the diet Recommended daily intake Recommended daily intake Micro less than 0.005% of body mass mg or μg per day Micro less than 0.005% of body mass mg or μg per day Vitamins and minerals Vitamins and minerals Needed to produce enzymes or other substances needed for health Needed to produce enzymes or other substances needed for health

3 Macronutrients For energy and structure For energy and structure Proteins, carbohydrates, lipids Proteins, carbohydrates, lipids Na,Mg,K,Ca,P,S and Cl Na,Mg,K,Ca,P,S and Cl

4 Dietary minerals Dietary minerals Major minerals–in bone Calcium, phosphate, magnesium Major minerals–in bone Calcium, phosphate, magnesium Major minerals–in electrolytes Sodium, potassium, chloride Major minerals–in electrolytes Sodium, potassium, chloride Minor minerals–in metalloproteins Iron, copper, manganese, iodine, cobalt, molybdenum, selenium, chromium, fluoride, zinc Minor minerals–in metalloproteins Iron, copper, manganese, iodine, cobalt, molybdenum, selenium, chromium, fluoride, zinc Trace minerals Nickel, silicon, vanadium, tin Trace minerals Nickel, silicon, vanadium, tin

5 Electrolyte results Electrolyte results Test Patient's Results Ref. RangeUnits Test Patient's Results Ref. RangeUnits TestPatient's ResultsRef. RangeUnits TestPatient's ResultsRef. RangeUnits BMP BMP Na L124 136-145mEq/L Na L124 136-145mEq/LL124 K H5.8 3.5-5.1mEq/L K H5.8 3.5-5.1mEq/LH5.8 CO2 25 23-29mEq/L CO2 25 23-29mEq/L Cl 101 98-107mEq/L Cl 101 98-107mEq/L Glucose H107 74-100mg/dL Glucose H107 74-100mg/dL Ca 10.1 8.6-10.2mg/dL Ca 10.1 8.6-10.2mg/dL BUN 17 8-23mg/dL BUN 17 8-23mg/dL Creatinine0.9 0.8-1.3mg/dL Creatinine0.9 0.8-1.3mg/dL Key: L=Abnormal Low, H=Abnormal High, WNL=Within Normal Limits, *=critical value Key: L=Abnormal Low, H=Abnormal High, WNL=Within Normal Limits, *=critical value

6 Vitamins Needed but not synthesized in the body Needed but not synthesized in the body Water or fat soluble Water or fat soluble Water -filtered out by kidneys and excreted Water -filtered out by kidneys and excreted Fat -absorbed and stored in fat tissues Fat -absorbed and stored in fat tissues Look at table 21 of the IB data booklet Look at table 21 of the IB data booklet

7 ADEK fat all others water

8 Look at data booklet Look at data booklet Vitamin A (retinol)structure Vitamin A (retinol)structure Fat Fat Important for vision at low light intensity Important for vision at low light intensity

9 Look at vitamin C (ascorbic acid) Look at vitamin C (ascorbic acid) Water Water Cofactor in enzyme reactions Cofactor in enzyme reactions Tissue regeneration after injury Tissue regeneration after injury

10 D (calciferol) D (calciferol) Fat Fat Similar in structure to cholesterol Similar in structure to cholesterol Uptake of Ca +2 by cells Uptake of Ca +2 by cells Healthy bones and teeth Healthy bones and teeth Get by sunlight or put in milk Get by sunlight or put in milk

11 Deficiency diseases Pick one for a report (in pairs) Pick one for a report (in pairs) Vitamin A, Iodine, iron, niacin, thiamin, vit. C, D, selenium, protein Vitamin A, Iodine, iron, niacin, thiamin, vit. C, D, selenium, protein Describe disease, pictures?, reasons, solutions Describe disease, pictures?, reasons, solutions

12 General summary of nutrient problems What is the problem in the USA? What is the problem in the USA? Worldwide causes and solutions Worldwide causes and solutions do questions 9 and 10 do questions 9 and 10

13 B.6 Hormones Communication systems Communication systems Nervous – electrochemical = quick Nervous – electrochemical = quick Endocrine – chemical messengers= slower Endocrine – chemical messengers= slower Different types of molecules Different types of molecules Produced in glands (no ducts) Produced in glands (no ducts) Receptors are target cells Receptors are target cells

14 Hormones

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16 Another report Another report ADH, thyroxine, aldosterone, adrenaline, insulin, estrogen, progesterone, testosterone ADH, thyroxine, aldosterone, adrenaline, insulin, estrogen, progesterone, testosterone Gland, type of molecule, target cells, functions Gland, type of molecule, target cells, functions

17 Look at your data booklet on hormones Look at your data booklet on hormones Compare cholesterol, estradiol(estrogen), progesterone, testosterone Compare cholesterol, estradiol(estrogen), progesterone, testosterone Alike and differences Alike and differences

18 Oral contraceptives Prevents ovulation Prevents ovulation Mixture of progesterone and estrogen Mixture of progesterone and estrogen Prevent release of follicle stimulating and luteinizing hormones Prevent release of follicle stimulating and luteinizing hormones No ovulation, simulates pregnancy No ovulation, simulates pregnancy

19 Use and abuse of steroids Hormone replacement therapy at menopause Hormone replacement therapy at menopause Male steroids (anabolic) androgens like testosterone Male steroids (anabolic) androgens like testosterone Enhance male characteristics Enhance male characteristics Overuse aggressive, liver cancer Overuse aggressive, liver cancer

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22 Do questions 11 and 12 Do questions 11 and 12

23 B.7 Enzymes Control system of the body Control system of the body Biological catalysts Biological catalysts

24 structure Globular proteins-several hundred amino acids Globular proteins-several hundred amino acids Tertiary and quaternary structures important Tertiary and quaternary structures important Co-factors binding non-protein molecules Co-factors binding non-protein molecules Organic called coenzymes inorganic metal ions Organic called coenzymes inorganic metal ions Examples vitamins Examples vitamins

25 Catalytic action Define enzyme Define enzyme Reactant is a substrate Reactant is a substrate Enzyme substrate complex Enzyme substrate complex Active site on the enzyme is a pocket or groove on the surface Active site on the enzyme is a pocket or groove on the surface Enzyme is larger than substrate Enzyme is larger than substrate

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28 Animation Animation Animation Another animation Another animation Another animation Another animation

29 saturation 3 things this tells us 3 things this tells us

30 Low conc. Rate relates to substate Low conc. Rate relates to substate As conc. Increases enzyme gets tied up As conc. Increases enzyme gets tied up High conc. Rate constant High conc. Rate constant

31 Michaelis-Menten Equation V max turnover number V max turnover number # molecules/second # molecules/second

32 Michaelis constant K m ½ V max ½ V max Specific pH and temp. Specific pH and temp. Units of concentration Units of concentration Low K m quick reaction constant rate Low K m quick reaction constant rate

33 Enzyme activity Temperature Temperature Increase rate as temp goes up Increase rate as temp goes up At a point the protein denatures At a point the protein denatures

34 Human optimum tends to be 37 o C Human optimum tends to be 37 o C Denaturation usually is irreversible Denaturation usually is irreversible Lowering temperature only causes deactivation Lowering temperature only causes deactivation High fevers can be fatal High fevers can be fatal

35 pH Changes affect the equilibrium positions Changes affect the equilibrium positions If it affects the R groups in amino acids it will alter the attractive ability thus influences the shape If it affects the R groups in amino acids it will alter the attractive ability thus influences the shape Each enzyme has an optimal pH Each enzyme has an optimal pH Extremes cause denaturation Extremes cause denaturation

36 For humans 7.4

37 Heavy metal ions Lead, copper, mercury and silver Lead, copper, mercury and silver Poisonous Poisonous React with SH groups on cysteine to make S-metal React with SH groups on cysteine to make S-metal Changes shape Changes shape

38 Chemical inhibitors Competitively at the active site Competitively at the active site Non-competitively at another area Non-competitively at another area

39 Competitive inhibitors

40 Takes a higher substrate concentration to reach V max Takes a higher substrate concentration to reach V max

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42 Chymotrpsin is an enzyme which hydrolyzes peptides at the carbonyl side of tyr or phe or trp (i.e. those that have an aromatic side chain. In the graphic on the left, the substrate and the irreversible inhibitor are shown in the active site pocket. In the case of the inhibitor the reaction starts in the same way as with the substrate, but the end result is that the inhibitor is covalently bonded to the histidine-57 in the active site and is not reversible Chymotrpsin is an enzyme which hydrolyzes peptides at the carbonyl side of tyr or phe or trp (i.e. those that have an aromatic side chain. In the graphic on the left, the substrate and the irreversible inhibitor are shown in the active site pocket. In the case of the inhibitor the reaction starts in the same way as with the substrate, but the end result is that the inhibitor is covalently bonded to the histidine-57 in the active site and is not reversible

43 Changes shape of enzyme Changes shape of enzyme Increasing concentration doesn’t help Increasing concentration doesn’t help Poisons DDT, cyanide and antibiotics Poisons DDT, cyanide and antibiotics Means of controlling metabolic activity in healthy cells Means of controlling metabolic activity in healthy cells Thermostat and heater Thermostat and heater

44 Enzymes vs. catalysts Enzymes are Enzymes are Specific Specific Reaction saturation Reaction saturation Speed up 1000 to 1000000 times Speed up 1000 to 1000000 times Can be inhibited Can be inhibited Very sensitive to environmental changes Very sensitive to environmental changes

45 Do questions 13 and 14 Do questions 13 and 14

46 B.8 Nucleic acids DNA and RNA DNA and RNA Information storage of genetics in the nucleus Information storage of genetics in the nucleus How did it begin? How did it begin?

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50 DNA must be stable DNA must be stable Contain a code Contain a code Be able to replicate Be able to replicate

51 Nucleic acid structure Polymers of nucleotides Polymers of nucleotides Three components Three components 1. pentose sugar 1. pentose sugar ribose ribose

52 Deoxyribose C 2 lacks an OH Deoxyribose C 2 lacks an OH

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54 2. Phosphate group PO 4 3+ PO 4 3+

55 3. Nitrogenous base Purine adenine (A) quanine (G) Purine adenine (A) quanine (G) Larger 2 fused rings Larger 2 fused rings Or pyrimidines smaller one ring Or pyrimidines smaller one ring

56 DNA bases

57 RNA Uracil replaces thymine one less CH 3 Uracil replaces thymine one less CH 3

58 PO 4 connects to the 5 carbon on the sugar, sugar connects from the 1 carbon

59 simplified

60 Joined together by condensation reactions Joined together by condensation reactions Phosphate on the 3 carbon of the adjoining sugar Phosphate on the 3 carbon of the adjoining sugar Called phosphodiester links Called phosphodiester links

61 polynucleotides

62 simplified

63 Putting it together Putting it together Putting it together Putting it together

64 Adenine pairs up with thymine (uracil in RNA) Adenine pairs up with thymine (uracil in RNA) Cytosine and guinine pair up Cytosine and guinine pair up Held together by hydrogen bonds Held together by hydrogen bonds

65 Double helix

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67 1 turn for each 10 nucleotides 1 turn for each 10 nucleotides Each side is upside down to each other Each side is upside down to each other Animation Animation Animation The dna game The dna game The dna game The dna game

68 RNA Single strand Single strand Ribose instead of d-ribose Ribose instead of d-ribose Uracil instead of thymine Uracil instead of thymine 3 types messenger (mRNA), transfer (tRNA), ribosomal (rRNA) 3 types messenger (mRNA), transfer (tRNA), ribosomal (rRNA)

69 transcription In the nucleus, Strands of DNA separate (unzip) In the nucleus, Strands of DNA separate (unzip) mRNA copies the code by lining up bases mRNA copies the code by lining up bases mRNA leaves nucleus mRNA leaves nucleus DNA zips up DNA zips up

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71 translation Happens in the ribosome Happens in the ribosome tRNA pulls in amino acids from the cytoplasm to make proteins tRNA pulls in amino acids from the cytoplasm to make proteins Codons every 3 nucleotide is the code for 1 amino acid Codons every 3 nucleotide is the code for 1 amino acid Activity for building a protein Activity for building a protein

72 Animation Animation Animation One more One more One more One more

73 DNA profiling Only 0.1% of DNA is different in humans Only 0.1% of DNA is different in humans 3 billion base pairs unique 3 billion base pairs unique

74 steps Obtain DNA from blood, saliva etc. Obtain DNA from blood, saliva etc. Cut into restriction enzymes Cut into restriction enzymes Make multiple copies Make multiple copies Use gel electrophoresis Use gel electrophoresis Irradiated for a autoradiogram Irradiated for a autoradiogram For identity of victims, suspects, paternity, relationships For identity of victims, suspects, paternity, relationships

75 Question 15

76 B.9 Respiration Release of energy Release of energy Glucose breakdown Glucose breakdown

77 aerobic Oxygen present Oxygen present Pyruvate oxidized to CO 2 and H 2 O Pyruvate oxidized to CO 2 and H 2 O Electron transport carriers-cytochromes Electron transport carriers-cytochromes animation animation animation

78 Anaerobic Without oxygen Without oxygen Glycolysis Glycolysis Glucose into pyruvate Glucose into pyruvate Coenzyme NAD + Coenzyme NAD + Forms lactic acid Forms lactic acid Only 2% of energy released Only 2% of energy released animation animation animation

79 Electron transport system involves Fe +2 to Fe +3 Electron transport system involves Fe +2 to Fe +3 CU +1 to Cu +2 CU +1 to Cu +2 Cytochrome Cytochrome Cytochrome oxidase passes e- to O 2 to make H 2 O Cytochrome oxidase passes e- to O 2 to make H 2 O

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82 Hemoglobbin O 2 bound to it O 2 bound to it Fe +2 stays in this state Fe +2 stays in this state Reversible oxy hemoglobbin Reversible oxy hemoglobbin

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85 Question 16 Question 16 Do the questions on page 541-545 in your textbook and 104 in your study booklet Do the questions on page 541-545 in your textbook and 104 in your study booklet


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