바이오사이언스 - Marks' Basic Medical Biochemistry Sixth, International Edition

Description:

Marks’ Basic Medical Biochemistry: A Clinical Approach, 6th Edition links biochemistry to physiology and pathophysiology, empowering students to confidently apply fundamental concepts to the practice of medicine — from diagnosing patients to recommending effective treatments. This proven, application-centered approach builds biochemical coverage around related clinical concepts to anchor students’ understanding to a clinical context from day one. Intuitively organized chapters center on hypothetical patient vignettes to emphasize clinical applications, and helpful icons, images, and review questions make complex concepts easier to grasp.
Cover
Title Page
Copyright
Preface to the Sixth Edition
How to Use This Book
Acknowledgments
Reviewers
Contents
Animation
Section I: Fuel Metabolism
1 Metabolic Fuels and Dietary Components
I. Dietary Fuels
A. Carbohydrates
B. Proteins
C. Fats
D. Alcohol
II. Body Fuel Stores
A. Fat
B. Glycogen
C. Protein
III. Daily Energy Expenditure
A. Basal Metabolic Rate
B. Physical Activity
C. Diet-Induced Thermogenesis
D. Calculations of Daily Energy Expenditure
E. Healthy Body Weight
F. Weight Gain and Loss
IV. Dietary Requirements
A. Carbohydrates
B. Essential Fatty Acids
C. Protein
D. Vitamins
E. Minerals
F. Water
V. Dietary Guidelines
A. General Recommendations
B. Carbohydrates
C. Fats
D. Proteins
E. Alcohol
F. Vitamins and Minerals
VI. Xenobiotics
Chapter 1: Review Questions
2 The Fed or Absorptive State
I. Digestion and Absorption
A. Carbohydrates
B. Proteins
C. Fats
II. Changes in Hormone Levels after a Meal
III. Fate of Glucose
A. Conversion to Glycogen, Triacylglycerols, and CO2 in the Liver
B. Glucose Metabolism in Other Tissues
IV. Lipoproteins
V. Amino Acids
VI. Summary of the Fed (Absorptive) State
Chapter 2: Review Questions
3 Fasting
I. The Fasting State
A. Blood Glucose and the Role of the Liver during Fasting
B. Role of Adipose Tissue during Fasting
C. Summary of the Metabolic Changes during a Brief Fast
II. Metabolic Changes during Prolonged Fasting
A. Role of Liver during Prolonged Fasting
B. Role of Adipose Tissue during Prolonged Fasting
Chapter 3: Review Questions
Section II: Chemical and Biologic Foundations of Biochemistry
4 Water, Acids, Bases, and Buffers
I. Water
A. Fluid Compartments in the Body
B. Hydrogen Bonds in Water
C. Electrolytes
D. Osmolality and Water Movement
II. Acids and Bases
A. The pH of Water
B. Strong and Weak Acids
III. Buffers
IV. Metabolic Acids and Buffers
A. The Bicarbonate Buffer System
B. Bicarbonate and Hemoglobin in Red Blood Cells
C. Intracellular pH
D. Urinary Hydrogen, Ammonium, and Phosphate Ions
E. Hydrochloric Acid
Chapter 4: Review Questions
5 Structures of the Major Compounds of the Body
I. Functional Groups on Biologic Compounds
A. Biologic Compounds
B. Functional Groups
C. Polarity of Bonds and Partial Charges
D. Nomenclature
II. Carbohydrates
A. Monosaccharides
B. Glycosides
III. Lipids
A. Fatty Acids
B. Acylglycerols
C. Phosphoacylglycerols
D. Sphingolipids
E. Steroids
IV. Nitrogen-Containing Compounds
A. Amino Acids
B. Nitrogen-Containing Ring Structures
V. Free Radicals
Chapter 5: Review Questions
6 Amino Acids in Proteins
I. General Structure of the Amino Acids
II. Classification of Amino Acid Side Chains
A. Nonpolar, Aliphatic Amino Acids
B. Aromatic Amino Acids
C. Aliphatic, Polar, Uncharged Amino Acids
D. Sulfur-Containing Amino Acids
E. The Acidic and Basic Amino Acids
III. Variations in Primary Structure
A. Polymorphism in Protein Structure
B. Tissue and Developmental Variations in Protein Structure
C. Species Variations in the Primary Structure of Insulin
A. Protein Families and Superfamilies
B. Creatine Kinase and Myocardial Infarctions
IV. Modified Amino Acids
A. Glycosylation
B. Fatty Acylation or Prenylation
C. Regulatory Modifications
D. Other Amino Acid Posttranslational Modifications
E. Selenocysteine
Chapter 6: Review Questions
7 Structure–Function Relationships in Proteins
I. General Characteristics of Three-Dimensional Structure
A. Descriptions of Protein Structure
B. Requirements of the Three-Dimensional Structure
II. The Three-Dimensional Structure of the Peptide Backbone
III. Secondary Structure
A. The α-Helix
B. β-Sheets
C. Nonrepetitive Secondary Structures
D. Patterns of Secondary Structure
IV. Tertiary Structure
A. Domains in the Tertiary Structure
B. Folds in Globular Proteins
C. The Solubility of Globular Proteins in an Aqueous Environment
D. Tertiary Structure of Transmembrane Proteins
V. Quaternary Structure
VI. Quantitation of Ligand Binding
VII. Structure–Function Relationships in Myoglobin and Hemoglobin
A. Oxygen Binding and Heme
B. Cooperativity of O2 Binding in Hemoglobin
C. Agents That Affect Oxygen Binding
C. Carbon Dioxide
VIII. Structure–Function Relationships in Immunoglobulins
IX. Protein Folding
A. Primary Structure Determines Folding
B. Fibrous Proteins—Collagen
C. Protein Denaturation
Chapter 7: Review Questions
8 Enzymes as Catalysts
I. The Enzyme-Catalyzed Reaction
A. The Active Site
B. Substrate-Binding Sites
C. The Transition-State Complex
II. Strategies for Catalysis
A. General Acid–Base Catalysis
II. Catalytic Mechanism of Chymotrypsin
A. The Reaction in the Absence of Enzyme
B. Catalytic Strategies in the Reaction Catalyzed by Chymotrypsin
C. Energy Diagram in the Presence of Chymotrypsin
B. Covalent Catalysis
C. Metal-Ion Catalysis
D. Catalysis by Approximation
E. Cofactor Catalysis
III. Functional Groups in Catalysis
A. Functional Groups on Amino Acid Side Chains
B. Coenzymes in Catalysis
C. Metal Ions in Catalysis (See Also Section II.C)
D. Noncatalytic Roles of Cofactors
IV. Optimal pH and Temperature
V. Mechanism-Based Inhibitors
A. Covalent Inhibitors
B. Transition-State Analogs and Compounds That Resemble Intermediate Stages of the Reaction
C. Heavy Metals
Chapter 8: Review Questions
9 Regulation of Enzymes
I. General Overview
II. Regulation by Substrate and Product Concentration
A. Velocity and Substrate Concentration
B. Reversible Inhibition within the Active Site
III. Regulation through Conformational Changes
A. Conformational Changes in Allosteric Enzymes
B. Conformational Changes from Covalent Modification
C. Conformational Changes Regulated by Protein–Protein Interactions
D. Proteolytic Cleavage
IV. Regulation through Changes in Amount of Enzyme
A. Regulated Enzyme Synthesis
B. Regulated Protein Degradation
V. Regulation of Metabolic Pathways
A. Principles of Pathway Regulation
Chapter 9: Review Questions
10 Cell Structure and Signaling by Chemical Messengers
I. Compartmentation in Cells
II. Plasma Membrane
A. Structure of the Plasma Membrane
B. Transport of Molecules across the Plasma Membrane
III. Lysosomes
IV. Mitochondria
V. Peroxisomes
VI. Nucleus
VII. Endoplasmic Reticulum
VIII. Golgi Complex
IX. Cytoskeleton
X. General Features of Chemical Messengers
A. General Features of Chemical Messenger Systems Applied to the Nicotinic Acetylcholine Receptor
B. Endocrine, Paracrine, Autocrine, and Juxtacrine Actions
C. Types of Chemical Messengers
XI. Intracellular Transcription Factor Receptors
A. Intracellular versus Plasma Membrane Receptors
B. The Steroid Hormone/Thyroid Hormone Superfamily of Receptors
XII. Plasma Membrane Receptors and Signal Transduction
A. Ion-Channel Receptors
B. Receptors That Are Kinases or That Bind Kinases
C. Heptahelical Receptors
D. Juxtacrine Signaling
XIII. Signal Termination
Chapter 10: Review Questions
11 Structure of the Nucleic Acids
I. DNA Structure
A. Location of DNA
B. Determination of the Structure of DNA
C. Concept of Base Pairing
D. DNA Strands Are Antiparallel
E. The Double Helix
F. Characteristics of DNA
II. Structure of Chromosomes
A. Size of DNA Molecules
B. Packaging of DNA
C. The Human Genome
III. Structure of RNA
A. General Features of RNA
B. Structure of mRNA
C. Structure of rRNA
D. Structure of tRNA
E. Other Types of RNA
Chapter 11: Review Questions
Section III: Gene Expression and the Synthesis of Proteins
12 Synthesis of DNA
I. DNA Synthesis in Prokaryotes
A. Bidirectional Replication
B. Semiconservative Replication
C. DNA Unwinding
D. DNA Polymerase Action
E. Base-Pairing Errors
F. RNA Primer Requirement
G. The Replication Fork
H. DNA Ligase
II. DNA Synthesis in Eukaryotes
A. Eukaryotic Cell Cycle
B. Points of Origin for Replication
C. Eukaryotic DNA Polymerases
D. The Eukaryotic Replication Complex
E. Replication at the Ends of Chromosomes
III. DNA Repair
A. Actions of Mutagens
B. Repair Mechanisms
IV. Genetic Rearrangements
A. General or Homologous Recombination
B. Translocations
C. Repair of Single- and Double-Strand Breaks in DNA
D. Transposable Elements
V. Reverse Transcriptase
Chapter 12: Review Questions
13 Transcription: Synthesis of RNA
I. Action of RNA Polymerase
II. Types of RNA Polymerases
A. Sequences of Genes
B. Recognition of Genes by RNA Polymerase
C. Promoter Regions of Genes for mRNA
III. Transcription of Bacterial Genes
IV. Transcription of Eukaryotic Genes
A. Synthesis of Eukaryotic mRNA
B. Synthesis of Eukaryotic rRNA
C. Synthesis of Eukaryotic tRNA
V. Differences in Size between Eukaryotic and Prokaryotic DNA
A. Diploid versus Haploid
B. Introns
C. Repetitive Sequences in Eukaryotic DNA
D. Summary of the Differences between Eukaryotic and Prokaryotic DNA and RNA
Chapter 13: Review Questions
14 Translation: Synthesis of Proteins
I. The Genetic Code
A. The Code Is Degenerate Yet Unambiguous
B. The Code Is Nonoverlapping
C. Relationship between mRNA and the Protein Product
II. Effects of Mutations
A. Point Mutations
B. Insertions, Deletions, and Frameshift Mutations
III. Formation of Aminoacyl-tRNA
IV. Process of Translation
A. Initiation of Translation
B. Elongation of Polypeptide Chains
C. Termination of Translation
V. Polysomes
VI. Processing of Proteins
VII. Posttranslational Modifications
VIII. Targeting of Proteins to Subcellular and Extracellular Locations

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상품정보고시

제품명	Marks' Basic Medical Biochemistry Sixth, International Edition
판매가격	75,000원
제조사	Wolters Kluwer