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Study Guide Basic Biochemistry Semester I 28 Desember 2015

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PLANNERS TEAM

No. NAME PHONE

1. Dr.dr. Desak Made Wihandani, M.Kes Head 081338776244

2. Dr.ret.nat.dr. Ni Nyoman Ayu Dewi Secretary 081337141506

3. Prof.dr. I Nyoman Agus Bagiada, SpBiok

Member 081338338611

4. dr. I Wayan Surudarma, M.Si Member 081338486589

5. dr. I Wayan Gede Sutadarma, M.Gizi, SpGK

Member 087862155380

6. dr. Ida Ayu Dewi Wiryanthini, M.Biomed

Member 08123625239

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~FACILITATORS ~

NO

NAME

GROUP

DEPT

PHONE

VENUE

1 Dr.dr. Elysanti Dwi Martadiani, Sp.Rad

1 Radiology 081805673099 2nd floor:

R.2.01 2 dr. Reni Widyastuti, S.Ked 2 Pharmacology 08174742501 2nd floor:

R.2.02 3 dr. Ni Ketut Putri Ariani, Sp.KJ 3 Psychiatry 082237817384 2nd floor:

R.2.03 4 dr I Gusti Agung Gede Utara

Hartawan, Sp.An, MARS

4 Anasthesi 08123868126 2nd floor:

R.2.04 5 dr. Ni Luh Ariwati 5 Parasitology 08123662311 2nd floor:

R.2.05 6 dr. I G Kamasan Nyoman

Arijana, M.Si, Med

6 Histology 08124665966 2nd floor:

R.2.06 7 Dr.dr. Ni Nyoman Sri

Budayanti, Sp.MK(K)

7 Microbiology 08553711398 2nd floor:

R.2.07 8 dr. Ni Nyoman Mahartini, Sp.PK 8 Clinical

Pathology

081337165577 2nd floor:

R.2.08 9 dr. I Wayan Sugiritama, M.Kes 9 Histology 08164732743 2nd floor:

R.2.21 10 dr. Ryan Saktika Mulyana,

M.Biomed, Sp.OG

10 Obgyn 082147087905 2nd floor:

R.2.22

ENGLISH CLASS

NO NAME GROUP DEPT PHONE VENUE

1 dr. Kunthi Yulianti, Sp.KF 1 Forensic 081338472005 2nd floor:

R.2.01 2 dr. I Nyoman Budi Hartawan,

M.Sc., Sp.A(K)

2 Pediatri 081353027973 2nd floor:

R.2.02 3 dr. I Wayan Surudarma, M.Si 3 Biochemistry 081338486589 2nd floor:

R.2.03 4 dr. I Gusti Ayu Artini, M.Sc 4 Pharmacology 08123650481 2nd floor:

R.2.04 5 dr. I Ketut Mariadi, Sp.PD 5 Interna 08123853700 2nd floor:

R.2.05 6 Dr.dr. Ni Made Linawati, M.Si 6 Histology 081337222567 2nd floor:

R.2.06 7 dr. I Nyoman Gede Wardana, M

Biomed

7 Anatomy 087860405625 2nd floor:

R.2.07 8 dr. I Wyn Subawa, Sp.OT 8 Orthopaedy 081338913087

081337096388

2nd floor:

R.2.08 9 Dr.rer.Nat. dr. Ni Nyoman Ayu

Dewi, M.Kes

9 Biochemistry 081337141506 2nd floor:

R.2.21 10 dr. I Komang Arimbawa, Sp.S 10 Neurology 081338226892 2nd floor:

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TIME TABLE BLOCK BASIC BIOCHEMISTRY (Dec, 28, 2015 - Jan, 15, 2016)

Day Date Topic Learning

situation EnglishClass RegularClass PIC

1 Monday, Elementer Lipid

Lecture Intro

Protein metabolism

Lecture 7

30, 2015 CarbohydrateMetabolism 1 Carbohydrate

Lipid metabolism 1

Lipid Metabolism 2

Lecture 5

4, 2016 Intermetabolismrelationship

Enzyme

2016 Bioenergetics Phosphorylation

Vitamin and Mineral

Free Radical & Anti oxidant

2016 Matrix extracelular Panel Discussion

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12 Thu, Jan, 14, 2016

Silent Day 13 Friday,

Jan,15, 2016

Evaluation Team

CARBOHYDRATE ELEMENTER

Abstract

Carbohydrates are major constituents of animal food and animal tissues. They are characterized by the type and number of monosaccharide residues in their molecules. Glucose is the most important carbohydrate in mammalian biochemistry because nearly all carbohydrate in food is converted to glucose for metabolism. Sugars have large numbers of stereoisomers because they contain several asymmetric carbon atoms. The monosaccharides include glucose, the “blood sugar”; and ribose, an important constituent of nucleotides and nucleic acids.

The disaccharides include maltose (glucosyl glucose), an intermediate in the digestion of starch; sucrose (glucosyl fructose), important as a dietary constituent containing fructose; and lactose (galactosyl glucose), in milk. Starch and glycogen are storage polymers of glucose in plants and animals, respectively. Starch is the major source of energy in the diet.

Complex carbohydrates contain other sugar derivatives such as amino sugars, uronic acids, and sialic acids. They include proteoglycans and glycosaminoglycans, associated with structural elements of the tis-sues; and glycoproteins, proteins containing attached oligosaccharide chains. They are found in many situations including the cell membrane.

Learning Task

1. Describes the characteristic of glucose, fructose and galactose 2. Describes the classification of carbohydrate

3. Identify the food sources of each carbohydrate 4. Describes the isomerism of glucose

5. Describes the characteristic of hexose and pentose sugar 6. Why the cell usually use glucose as a fuel

7. Describe the characteristic of glycogen and starch 8. Describes the characteristic of carbohydrate as a fiber

LIPID ELEMENTER

Abstract

Lipids have the common property of being relatively insoluble in water (hydrophobic) but soluble in non-polar solvents. Amphipathic lipids also contain one or more polar groups, making them suitable as constituents of membranes at lipid : water interfaces. The lipids of major physiologic significance are fatty acids and their esters, together with cholesterol and other steroids.

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pharmacologically active compounds known as prostaglandins, thromboxanes, leukotrienes, and lipoxins.

The esters of glycerol are quantitatively the most significant lipids, represented by triacylglycerol (“fat”), a major constituent of lipoproteins and the storage form of lipid in adipose tissue. Phosphoacylglycerols are amphipathic lipids and have important roles—as major constituents of membranes and the outer layer of lipoproteins, as surfactant in the lung, as precursors of second messengers, and as constituents of nervous tissue. Glycolipids are also important constituents of nervous tissue such as brain and the outer leaflet of the cell membrane, where they contribute to the carbo-hydrates on the cell surface.

Cholesterol, an amphipathic lipid, is an important component of membranes. It is the parent molecule from which all other steroids in the body, including major hormones such as the adrenocortical and sex hormones, D vitamins, and bile acids, are synthesized. Peroxidation of lipids containing polyunsaturated fatty acids leads to generation of free radicals that may damage tissues and cause disease.

Learning Task

1. Describes the characteristic of lipid 2. Describes the classification of lipid

3. Identify the nomenclature methods of lipid

4. Describes the different between saturated fatty acids and unsaturated fatty acids 5. Identify the food sources of each fatty acids

6. Describes the characteristic of essential fatty acids 7. Describes the different between cis- and trans- fatty acids 8. Describes the characteristic of cholesterol

9. Describe the characteristic of lipoprotein 10. What or how is the lipid peroxidation occur

PROTEIN ELEMENTER & METABOLISM

Abstract

Proteins play an important role in virtually every life process; proteins display a diverse function such as regulate metabolism (hormones), play a role in gas transport (hemoglobin), against pathogens (immunoglobulin), etc. Protein consists of amino acids that are joined together by peptide bonds. Protein has complexity of structures and can be found in primary, secondary, tertiary and quaternary structure. Amino acids can be classified based on chemical properties or on nutritional aspect. Amino acids are not stored by our body. Amino acids are obtained from the diet, synthesized de novo, or produced from normal protein degradation. Excess of amino acids in our body are rapidly degraded. Catabolism of amino acids involves: i) the removal of the α-amino groups, forming free ammonia which is used in the synthesis of urea (urea cycle); this is the important route of nitrogen disposal, ii) catabolism of carbon skeletons that are converted to common intermediates of energy production, depending on the type of amino acids.

Mutation of gene generally results in abnormal proteins that may lead to so called inborn errors of metabolism which most of the diseases are rare. The most important disease of amino acid metabolism is phenylketonuria (PKU) because it is relatively common and responds to dietary treatment.

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1. What is protein and what is amino acid? What is peptide bond? 2. Describe and give example of quaternary protein

3. Describe amino acid classification

4. Describe the fate of carbon skeletons of amino acids 5. Describe urea cycle

6. Describe the underlying cause of PKU, maple syrup urine disease, homocystinuria, albinism and alkaptonuria

CARBOHYDRATE METABOLISM

Abstract

The simple forms of carbohydrate and has importance role is glucose. There are several transporter for glucose to enter the cell. The clinical importance of glucose is to provide energy for body by glycolysis. Glucose catabolism and generate energy. Excess of glucose will change in to glycogen and stores in liver and muscle which can turn again in to glucose.

Glucose also entering pentose pathway “shunt” and produce ribose. It also entering intermediate metabolism called Tricarboxylic Acid Cycle and produce energy.

Learning Task:

1. Explain what happened during investment stage, splitting stage and yield stage on glycolisis.

2. How many ATP produced froma aerob glycolysis?

3. Explain about glycogenesis, glycogenolysis and hormonal control of glycogenolysis!

4. Where is Pentosa phosphate pathway started and what are the main products? Explain why its called “shunt”?

5. How many ATP produced from one molecule glucose metabolized at Kreb’s cycle?

ENZYME

Abstract

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although not directly able to classify the class of enzymes. IUBS system has clearly can classify classes of enzymes and until now has been known six classes of enzymes include: Oxydoreductase, Transferase, Hydrolase, Lyase, Isomerase and Lygase.

Learning Tasks

1. What is enzyme, koenzyme and holoenzyme

2. What is non protein catalyst

3.

What is prosthetic groups

4. What is enzyme kinetics

5. Describe the mechanism of enzyme working

6. Describe the function of enzyme in metabolisms reaction.

7. Explain definition and mechanism of competitive inhibitors

8. What is a non-functional plasma enzyme?. Give five examples

9. Explain about classification of enzyme based on IUBS system.

10. Why digestive enzymes are classified into hydrolase?.

BIOENERGETICS

Abstract

Bioenergetics describes the transfer and utilization of energy in biologic systems. It makes use of a few basic ideas from the field of thermo-dynamics, particularly the concept of free energy. Changes in free energy (G) provide a measure of the energetic feasibility of a chemical reaction and can, therefore, allow prediction of whether a reaction or process can take place. Bioenergetics concerns only the initial and final energy states of reaction components, not the mechanism or how much time is needed for the chemical change to take place. The direction and extent to which a chemical reaction proceeds is determined by the degree to which two factors change during the reaction. These are enthalpy (H, a measure of the change in heat content of the reactants and products) and entropy (S, a measure of the change in randomness or disorder of reactants and products). Enthalpy and entropy can be used to define a third quantity, free energy (G), which predicts the direction in which a reaction will spontaneously proceed. The change in free energy is represented in two ways, G and G0. ΔG represents the change in free energy and, thus, the direction of a reaction at any specified concentration of products and reactants. This contrasts with the standard free energy change, G0, which is the energy change when reactants and products are at a concentration of 1 mol/L.

Learning Task

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2. Explain the free energy, enthalpy and entropy concept! 3. Describe the structure of ATP!

4. How does ATP as an energy carrier? 5. What is coupling reaction?

THE ELECTRON TRANSPORT CHAIN & OXIDATIVE PHOSPHORYLATION

Abstract

Energy-rich molecules, such as glucose, are metab olized by a series of oxidation reactions ultimately yielding CO2 and water. The metabolic intermediates of these reactions donate electrons to specific coenzymes nicotinamide adenine dinucleotide (NAD+) and flavin adenine dinucleotide (FAD) to form the energy-rich reduced coenzymes, NADH and FADH2. These reduced coenzymes can, in turn, each donate a pair of electrons to a specialized set of electron carriers, collectively called the electron transport chain. As electrons are passed down the electron transport chain, they lose much of their free energy. Part of this energy can be captured and stored by the production of ATP from ADP and inorganic phosphate (Pi). This process is called oxidative phosphorylation. The chemiosmotic hypothesis (also known as the Mitchell hypothesis) explains how the free energy generated by the transport of electrons

by the electron transport chain is used to produce ATP from ADP + Pi.

Learning Task

1. What is Electron Transport Chain?

2. Discribe the transport of electron on the mitochondrial electron transport system! 3. What is Oxidative phosphorylation?

4. Discribe the structure of the ATP sinthase!

5. Explain The Chemyosmotic Hypothesis of ATP synthesis! 6. Mention few examples of Inhibitors and uncouplers?

VITAMIN AND MINERAL Abstract

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(retinol), present in carnivorous diets, and the provitamin (β-carotene), found in plants, form retinaldehyde, utilized in vision, and retinoic acid, which acts in the control of gene expression. Vitamin D is a steroid prohormone yielding the active hormone derivative calcitriol, which regulates calcium and phosphate metabolism. Vitamin D deficiency leads to rickets and osteomalacia.

Vitamin E (tocopherol) is the most important antioxidant in the body, acting in the lipid phase of

membranes and protecting against the effects of free radicals. Vitamin K functions as cofactor to a carboxylase that acts on glutamate residues of clotting factor precursor proteins to enable them to chelate calcium. The water-soluble vitamins of the B complex act as enzyme cofactors. Thiamin is a cofactor in oxidative decarboxylation of α-keto acids and of transketolase in the pentose phosphate pathway. Riboflavin and niacin are important cofactors in oxidoreduction reactions, respectively present in flavoprotein enzymes and in NAD and NADP.

Pantothenic acid is present in coenzyme A and acylcarrier protein, which act as carriers for acyl groupsin metabolic reactions. Pyridoxine, as pyridoxal phosphate, is the coenzyme for several enzymes of amino acid metabolism, including the aminotransferases, and of glycogen phosphorylase. Biotin is the

coenzyme for several carboxylase enzymes. Besides other functions, vitamin B12 and folic acid take part in providing one-carbon residues for DNA synthesis, deficiency resulting in megaloblastic anemia. Vitamin C is a water-soluble antioxidant that maintains vitamin E and many metal cofactors in the reduced state.

Inorganic mineral elements that have a function in the body must be provided in the diet. When insufficient, deficiency symptoms may arise, and if present in excess they may be toxic.

FREE RADICAL & ANTI OXIDANT Abstract

A free radical is an atom or molecule or ion that has a single unpaired electron in an outer shell. Free radicals are highly reactive and have the potential to cause damage to cells, including damage that may lead to cancer. Free radicals are formed naturally in the body. Some free radicals arise normally during metabolism. Sometimes the body immune system cells purposefully create them to neutralize viruses and bacteria. However, environmental factors such as pollution, radiation, cigarette smoke and herbicides can also spawn free radicals. While a few free radicals such as melanin are not chemically reactive, most biologically-relevant free radicals are highly reactive.

Antioxidants are chemicals that block the activity of free radicals. Normally, the body can handle free radicals, but if antioxidants are unavailable, or if the free-radical production becomes excessive, damage can occur that's called oxidative stress. The vitamins C and E, are thought to protect the body against the destructive effects of free radicals. Antioxidants neutralize free radicals by donating one of their own electrons, ending the electron-"stealing" reaction. The antioxidant nutrients themselves do not become free radicals by donating an electron because they are stable in either form. They act as scavengers, helping to prevent cell and tissue damage that could lead to cellular damage and disease.

Learning Task

1. What is the diffrece between free radical and oxidant?

2. Classify free radical based on their sources!

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4. Give 3 of biological markers to detect oksidatif damage by free radical

5. Give 3 examples of the beneficial of free radical

6. Differentiate between internal and external antioxidant

7. Give some example of external anti oxidant and internal antioxidant

EXTRACELLULAR MATRIX

Abstract

Extra celuler Matrix also called connective tissue, placed in extra cell space. Which most of it formed from protein. Amount, distribution and component depend on structure and function. Differentiation of the composition and turnover related to chronic disease.

Learning Task

1. What is ECM?

2. How was the differentiation of ECM?

CASE

A 35-year-old man employee has 90 kg of weight, 165 cm of height and 110 cm of abdominal circumference. He always has his meals in a canteen next to his office. Food he eats every day is quite similar. He eats twice a day, at 2pm and 8pm. His daily meals are described as follows: i) for breakfast, he sometimes drinks instant coffee and eats fried bananas, ii) for lunch, he always takes rice, crispy-skin fried chicken, fried tofu, fried tempe, soup of vegetables nodes which contains pumpkin, baby corn, and peanuts, iii) for dinner, he eats rice with fried or grilled chicken, raw cucumber and basil. He has almost no exercise/sports because of his busy works. Recently, he complains of fatique and weakness.

Learning Task SGD 1

1. Mention and explain content of macronutrient in the case! 2. Mention and explain the missing nutrients in the case 3. Are there essential amino acids within the food? Explain! 4. Mention and explain vitamins content of his meal! 5. Mention and explain minerals content of his meal! 6. Mention and explain fibers content of his meal!

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JADWAL PRAKTIKUM BIOKIMIA UNTUK KELAS REGULER

TANGGAL TEMPAT WAKTU NIM MAHASISWA INSTRUKTUR

11 Januari 2016 Lab. Bersama Lt

4

08.00-09.00 1502005001 s/d

1502005029

Sutadarma dan Supadmanaba

Lab. Bersama Lt

4

09.00-10.00 1502005053 s/d

1502005070

Sutadarma dan Supadmanaba

Lab. Bersama Lt

4

10.00-11.00 1502005120 s/d

1502005144

Sutadarma

Lab. Bersama Lt

4

11.00-12.00 1502005181 s/d

1502005223

Sutadarma

Lab Farmasi Lt

1

08.00-09.00 1502005030 s/d

1502005051

Dewi Wiryanthini

Lab Farmasi Lt

1

09.00-10.00 1502005071 s/d

1502005118

Dewi Wiryanthini

Lab Farmasi Lt

1

10.00-11.00 1502005145 s/d

1502005178

Dewi Wiryanthini

Lab Farmasi Lt

1

11.00-12.00 1502005235 s/d

1502005262

(12)

JADWAL PRAKTIKUM BIOKIMIA UNTUK ENGLISH CLASS

TANGGAL TEMPAT WAKTU NIM MAHASISWA INSTRUKTUR

11 Januari 2016 Lab. Bersama Lt

4

12.00-13.00 1502005004 s/d

1502005033

Sutadarma

Lab. Bersama Lt

4

13.00-14.00 1502005095 s/d

1502005135

Sutadarma

Lab. Bersama Lt

4

14.00-15.00 1502005172 s/d

1502005189

Sutadarma

Lab. Bersama Lt

4

15.00-16.00 1502005205 s/d

1502005231

Sutadarma

Lab Farmasi Lt

1

12.00-13.00 1502005035 s/d

1502005094

Dewi Wiryanthini dan Supadamanaba

Lab Farmasi Lt

1

13.00-14.00 1502005139 s/d

1502005171

Dewi Wiryanthini dan Supadamanaba

Lab Farmasi Lt

1

14.00-15.00 1502005190 s/d

1502005204

Dewi Wiryanthini

Lab Farmasi Lt

1

15.00-16.00 1502005234 s/d

1502005263

(13)

JADWAL PRAKTIKUM BIOKIMIA UNTUK KELAS REGULER

TANGGAL TEMPAT WAKTU NIM MAHASISWA INSTRUKTUR

12 Januari 2016 Lab. Bersama Lt 4

08.00-09.00 1502005001 s/d 1502005029

Desak Wihandani dan Supadmanaba Lab. Bersama Lt

4

09.00-10.00 1502005053 s/d 1502005070

Desak Wihandani dan Supadmanaba Lab. Bersama Lt

4

10.00-11.00 1502005120 s/d

1502005144

Agus Bagiada dan Supadmanaba

Lab. Bersama Lt

4

11.00-12.00 1502005181 s/d

1502005223

Agus Bagiada dan Supadmanaba

Lab Farmasi Lt

1

08.00-09.00 1502005030 s/d

1502005051

Tianing

Lab Farmasi Lt

1

09.00-10.00 1502005071 s/d

1502005118

Tianing

Lab Farmasi Lt

1

10.00-11.00 1502005145 s/d

1502005178

Ayu Dewi

Lab Farmasi Lt

1

11.00-12.00 1502005235 s/d

1502005262

(14)

JADWAL PRAKTIKUM BIOKIMIA UNTUK ENGLISH CLASS

TANGGAL TEMPAT WAKTU NIM MAHASISWA INSTRUKTUR

12 Januari 2016 Lab. Bersama Lt

4

12.00-13.00 1502005004 s/d

1502005033

Surudarma

Lab. Bersama Lt

4

13.00-14.00 1502005095 s/d

1502005135

Surudarma

Lab. Bersama Lt

4

14.00-15.00 1502005172 s/d

1502005189

Tianing

Lab. Bersama Lt

4

15.00-16.00 1502005205 s/d

1502005231

Tianing

Lab Farmasi Lt

1

12.00-13.00 1502005035 s/d

1502005094

Agus Bagiada dan Supadmanaba

Lab Farmasi Lt

1

13.00-14.00 1502005139 s/d

1502005171

Agus Bagiada dan Supadmanaba

Lab Farmasi Lt

1

14.00-15.00 1502005190 s/d

1502005204

Ayu Dewi

Lab Farmasi Lt

1

15.00-16.00 1502005234 s/d

1502005263

(15)

JADWAL PRAKTIKUM BIOKIMIA UNTUK KELAS REGULER

TANGGAL TEMPAT WAKTU NIM MAHASISWA INSTRUKTUR

13 Januari 2016 Lab. Bersama Lt

4

08.00-09.00 1502005001 s/d

1502005029

Agus Bagiada dan Supadmanaba

Lab. Bersama Lt

4

09.00-10.00 1502005053 s/d

1502005070

Agus Bagiada dan Supadmanaba

Lab. Bersama Lt

4

10.00-11.00 1502005120 s/d

1502005144

Ayu Dewi

Lab. Bersama Lt

4

11.00-12.00 1502005181 s/d

1502005223

Ayu Dewi

Lab Farmasi Lt

1

08.00-09.00 1502005030 s/d

1502005051

Desak Wihandani

Lab Farmasi Lt

1

09.00-10.00 1502005071 s/d

1502005118

Desak Wihandani

Lab Farmasi Lt

1

10.00-11.00 1502005145 s/d

1502005178

Desak Wihandani

Lab Farmasi Lt

1

11.00-12.00 1502005235 s/d

1502005262

Surudarma

JADWAL PRAKTIKUM BIOKIMIA UNTUK ENGLISH CLASS

TANGGAL TEMPAT WAKTU NIM MAHASISWA INSTRUKTUR

13 Januari 2016 Lab. Bersama Lt

4

12.00-13.00 1502005004 s/d

1502005033

Surudarma

Lab. Bersama Lt

4

13.00-14.00 1502005095 s/d

1502005135

Ayu Dewi

Lab. Bersama Lt

4

14.00-15.00 1502005172 s/d

1502005189

Surudarma

Lab. Bersama Lt

4

15.00-16.00 1502005205 s/d

1502005231

(16)

Lab Farmasi Lt

1

12.00-13.00 1502005035 s/d

1502005094

Tianing

Lab Farmasi Lt

1

13.00-14.00 1502005139 s/d

1502005171

Tianing

Lab Farmasi Lt

1

14.00-15.00 1502005190 s/d

1502005204

Desak Wihandani dan Supadmanaba

Lab Farmasi Lt

1

15.00-16.00 1502005234 s/d

1502005263

Desak Wihandani dan Supadmanaba

Catatan:

Mbak Amy bertugas pagi di Lab lantai 4, siang di Lab lantai 1

CURRICULUM MAP

Smstr Program or curriculum blocks

10 Senior Clerkship

9 Senior Clerkship

8 Senior Clerkship

7 Health System-based Practice

(3 weeks)

Special topics : Health Ergonomic & Health Environment

(2 weeks)

Elective StudyIV (evaluation)

6 The Cardiovascular System and Disorders

The Urinary System and Disorders (3 weeks)

BCS (1 weeks)

The Reproductive System and Disorders (4 weeks)

The Respiratory System and Disorders (4 weeks)

BCS (1 weeks)

The skin & hearing system

& disorders (3 weeks)

BCS (1 weeks)

Special Topic : - Palliative med - Complemnt & Alternative Med.

& hepatobiliary systems

The Endocrine System,

Clinical Nutrition and Disorders

The Visual

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connective tissue

Metabolism and Disorders

BCS (1weeks)

3 Basic microbiology & parasitology (3 weeks)

Immune system & disorders (2 weeks)

BCS (1 weeks)

Hematologic system & disorder & clinical oncology (3 weeks)

BCS (1 weeks)

Special Topic - sexology & anti aging l medicine & drug etics

(1 weeks)

19 weeks

2 Medicalcommunication (3 weeks)

Basic pharmacology (2 weeks)

BCS (1 weeks)

Medical Professionalism (2 weeks) + medical ethic (1 weeks) Basic Anatomy Pathology & Clinical pathology (3 weeks)

BCS (1 weeks)

Behavior Change and disorders

(3 weeks)

BCS (1 weeks)

Elective Study I

(2 weeks) 19 weeks

1 Studium Generale and

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