Wondershare EdrawMind
EdrawMindBiochemistry
MindMap Gallery Biochemistry
- 4
Biochemistry
The biochemistry outline helps everyone to better grasp the knowledge points, review the knowledge, sort out the knowledge clearly, and is very practical. It is an indispensable learning assistant and is worth collecting.
Edited at 2025-01-04 23:16:23- Rumi 10 spiritual high-dimensional awakenings
Rumi: 10 dimensions of spiritual awakening. When you stop looking for yourself, you will find the entire universe because what you are looking for is also looking for you. Anything you do persevere every day can open a door to the depths of your spirit. In silence, I slipped into the secret realm, and I enjoyed everything to observe the magic around me, and didn't make any noise. Why do you like to crawl when you are born with wings? The soul has its own ears and can hear things that the mind cannot understand. Seek inward for the answer to everything, everything in the universe is in you. Lovers do not end up meeting somewhere, and there is no parting in this world. A wound is where light enters your heart.
- Pathophysiology - Heart failure
Chronic heart failure is not just a problem of the speed of heart rate! It is caused by the decrease in myocardial contraction and diastolic function, which leads to insufficient cardiac output, which in turn causes congestion in the pulmonary circulation and congestion in the systemic circulation. From causes, inducement to compensation mechanisms, the pathophysiological processes of heart failure are complex and diverse. By controlling edema, reducing the heart's front and afterload, improving cardiac comfort function, and preventing and treating basic causes, we can effectively respond to this challenge. Only by understanding the mechanisms and clinical manifestations of heart failure and mastering prevention and treatment strategies can we better protect heart health.
- Pathophysiology - ischemia - reperfusion injury
Ischemia-reperfusion injury is a phenomenon that cellular function and metabolic disorders and structural damage will worsen after organs or tissues restore blood supply. Its main mechanisms include increased free radical generation, calcium overload, and the role of microvascular and leukocytes. The heart and brain are common damaged organs, manifested as changes in myocardial metabolism and ultrastructural changes, decreased cardiac function, etc. Prevention and control measures include removing free radicals, reducing calcium overload, improving metabolism and controlling reperfusion conditions, such as low sodium, low temperature, low pressure, etc. Understanding these mechanisms can help develop effective treatment options and alleviate ischemic injury.
Biochemistry
- Rumi 10 spiritual high-dimensional awakenings
Rumi: 10 dimensions of spiritual awakening. When you stop looking for yourself, you will find the entire universe because what you are looking for is also looking for you. Anything you do persevere every day can open a door to the depths of your spirit. In silence, I slipped into the secret realm, and I enjoyed everything to observe the magic around me, and didn't make any noise. Why do you like to crawl when you are born with wings? The soul has its own ears and can hear things that the mind cannot understand. Seek inward for the answer to everything, everything in the universe is in you. Lovers do not end up meeting somewhere, and there is no parting in this world. A wound is where light enters your heart.
- Pathophysiology - Heart failure
Chronic heart failure is not just a problem of the speed of heart rate! It is caused by the decrease in myocardial contraction and diastolic function, which leads to insufficient cardiac output, which in turn causes congestion in the pulmonary circulation and congestion in the systemic circulation. From causes, inducement to compensation mechanisms, the pathophysiological processes of heart failure are complex and diverse. By controlling edema, reducing the heart's front and afterload, improving cardiac comfort function, and preventing and treating basic causes, we can effectively respond to this challenge. Only by understanding the mechanisms and clinical manifestations of heart failure and mastering prevention and treatment strategies can we better protect heart health.
- Pathophysiology - ischemia - reperfusion injury
Ischemia-reperfusion injury is a phenomenon that cellular function and metabolic disorders and structural damage will worsen after organs or tissues restore blood supply. Its main mechanisms include increased free radical generation, calcium overload, and the role of microvascular and leukocytes. The heart and brain are common damaged organs, manifested as changes in myocardial metabolism and ultrastructural changes, decreased cardiac function, etc. Prevention and control measures include removing free radicals, reducing calcium overload, improving metabolism and controlling reperfusion conditions, such as low sodium, low temperature, low pressure, etc. Understanding these mechanisms can help develop effective treatment options and alleviate ischemic injury.
- Recommended to you
- Outline
Biochemistry
1. Structure and function of proteins
Amino acids and peptides
The structure of amino acids
The basic structure of protein is amino acid
Classification of amino acids
Essential amino acids: The idiot comes to the dormitory to dry his feet
Sub-theme
Peptide bonds and peptide chains
The peptide bonds in polypeptides are essentially amide bonds
The structure of protein
First-level structure
Peptide bonds
Secondary structure
α-helical, β-sheet, β-turning angle, Ω ring
Hydrogen bonding
Three-level structure
Hydrophobic bonds, salt bonds, hydrogen bonds, van der Waals bonds
Level 4 structure
Agent
Hydrogen bonds, ion bonds
The relationship between protein structure and function
The relationship between primary structure and functional of proteins
Sickle anemia: glutamate-valine
The relationship between advanced structure and function of proteins
Hb component in adult red blood cells: α2β2
Physical and chemical properties of proteins
Isoelectric point of protein
Precipitation and denaturation of proteins
Protein denaturation: destruction of disulfide bonds and non-covalent bonds, without involving primary structures
The precipitated protein does not necessarily degenerate
2. Structure and function of nucleic acids
Chemical composition of nucleic acids
Classification of nucleic acids
DNA
AGCT
RNA
AGCU
Nucleotides are the basic constituent units of nucleic acids
Nucleoside (glycosidic bond)
Nucleoside-acid (phospholipid bond)
between nucleotides (3', 5'-phosphodiester bonds)
The primary structure of nucleic acid
Structure and function of DNA
DNA base composition law (Chargaff law)
A=T, G=C
Genetic specificity of DNA base composition
DNA base composition is unorganized or organ-specific
The base composition in an organism is generally not affected by age, growth status, nutritional status and environmental factors.
The primary structure of DNA
The secondary structure of DNA (Double helix structure model of DNA)
The ratio of A G to C T is 1
Double-stranded, parallel, paired, complementary, reverse
Advanced structure of DNA
DNA function
Template for gene replication transcription
Information basis for individual life activities
Degeneration of DNA and its applications
UV absorption characteristics of nucleic acids
260nm maximum absorption peak
DNA degeneration
Hydrogen bond breakage
DNA regeneration
DNA denaturation is reversible
Nucleic acid hybridization
Structure and function of RNA
Types and functions of RNA
mRNA
Eukaryotic organisms
Template function
Prokaryotic organisms
tRNA
Transport function
The smallest molecular weight and the most rare bases
rRNA
The most in-cell content
Participate in protein synthesis
3. Enzyme and enzymatic reaction
Catalytic action of enzymes
Molecular structure and catalytic action of enzymes
The molecular composition of enzymes
Simple enzyme
Binding enzymes
Enzyme protein: the specificity of the reaction
Cofactor: Determines the type and properties of the reaction
Classification of cofactors
Coenzyme
Auxiliary
The activity center of enzyme
Characteristics of enzyme-promoting reaction
Extremely high catalytic efficiency
High specificity
Enzymatic reactions are adjustable
Enzyme-substrate complex
Induction fit
Enzyme cofactors
The relationship between vitamins and coenzymes
The effect of coenzyme
The role of metal ions
Enzymatic reaction kinetics
Km and Vmax
Km has nothing to do with enzyme concentration
For the same substrate, different enzymes have different Km values
Km indicates the affinity of the enzyme. The smaller the Km value, the greater the affinity.
Vmax is the reaction rate when the enzyme is completely saturated by the substrate, which is proportional to the enzyme concentration.
Optimal pH and optimal temperature
Optimal pH
Pepsin 1.8
Glycerinase 9.8
Trypsin 7.8
Optimal temperature
35-40℃
Effect of enzyme concentration on enzymatic reaction rate
Straight line relationship, proportional
Inhibitors and activators
Irreversible suppression
Inhibiting cholinesterase
Organophosphorus pesticides
The thiol group that inhibits enzymes
Heavy metal ions
Louis Morale
Reversibility inhibition
Competitive inhibitory effect
Km enlargement
Noncompetitive inhibitory effect
Vmax reduction
Anticompetitive inhibitory effect
Km decreases, Vmax decreases
Activator
Mostly metal ions
Regulation of enzyme activity
Allomorphic adjustment
Chemical modification regulation
Commonly modified by phosphorylation
zymogen activation
Prothrombin
Isozyme
Ribozyme
RNA with catalytic activity
4. Vitamin
Fat-soluble vitamins
Vitamin A
Night blindness, dry eyes
Vitamin D
Rickets, chondrosis
Vitamin E
Hemolytic anemia
Neurological function
Vitamin K
Bleeding
Water-soluble vitamins
Vitamin B1
Bear foot disease, peripheral neuritis
Vitamin B2
Angular stomatitis, glossopharynx, cheilitis
Vitamin B6
Vitamin B12
Giant red, nerve demyelination
Vitamin PP
Peptic disease
Vitamin C
Scurvy
Pantothenic acid
Folic acid
Giant young red
Biotin
5. Sugar metabolism
Catabolic metabolism of sugar
Anaerobic fermentation of sugar (glycolysis)
2ATP per molecule of glucose
Basic ways
The first stage (pathway) glucose decomposition into pyruvate
The second stage (process) reduction of pyruvate to lactose
Key enzymes
Hexokinase
Phosphofructokinase-1
Pyruvate kinase
Physiological significance
The only way to supply red blood cells
Aerobic oxidation of sugar
30/32 ATP per molecule of glucose
Basic ways
Phase 1
Same glycolysis
Phase 2
Pyruvate production of acetylCOA
Stage 3
AcetylCOA enters the tricarboxylic acid cycle and is completely oxidized
Key enzymes
Hexokinase
6-Phosophyrofructokinase-1
Pyruvate kinase
Pyruvate dehydrogenase complex
Citrate synthase
Isocitrate dehydrogenase
α-ketoglutarate dehydrogenase complex
Physiological significance
Provide energy
Intermediate products
Metabolic link
Sub-theme
Physiological significance of tricarboxylic acid cycle
The final oxidation pathway of sugar, fat and protein
Key enzymes
Citrate synthase
Isocitrate dehydrogenase
α-ketoglutarate dehydrogenase complex
Pentose phosphate pathway
Key enzymes
Grape-6-phosphate dehydrogenase
(Labor) Broad bean disease
Important products
Physiological significance
Provide ribose for the biosynthesis of nucleic acids
Provide NADPH as a hydrogen donor to participate in various metabolic reactions
Synthesis and decomposition of glycogen
Liver glycogen synthesis
Key enzyme: glycoprokaryase
Reserve glycogen
Liver glycogen breakdown
Key enzyme: glycogen phosphorylase
Maintain blood sugar
Glycogenesis
Key enzymes
Pyruvate carboxylase (most important)
Phosphoenolpyruvate carboxykinase
Fructose Biphosphatase-1
Grape-6-phosphatase
Basic ways
Physiological significance
Maintain constant blood sugar concentration
Supplement or restore liver glycogen reserves
Maintain acid-base balance
Lactate cycle
Cyclic process
Physiological significance
Recycle energy from lactic acid to avoid acidosis
Energy consumption, 2 molecules of lactic acid are heterogeneously generated glucose consume 6ATP
Blood sugar and its regulation
Blood sugar concentration
Normal 3.9-6.0mmol/L
source
Go to
Regulation of blood sugar levels
insulin
Glucagon
Glucocorticoid
6. Bio-oxidation
Oxidative phosphorylation
Two breathing chains
NADH oxidative respiratory chain
FADH2 oxidative respiratory chain (succinic acid oxidative respiratory chain)
Coupling sites for oxidative phosphorylation of respiratory chains
The P/O ratio of the NADH oxidative respiratory chain is about 2.5
The P/O ratio of succinic acid oxidative respiratory chain is about 1.5
ATP synthase
F1 hydrophilic part
F0 hydrophobic part
Regulation of oxidative phosphorylation and its influencing factors
Oxidative phosphorylation inhibitors
Respiratory chain inhibitors
Uncoupling agent
Dinitrobenol
ATP synthase inhibitor
The regulatory effect of ADP
The regulatory effect of thyroid hormone
Mitochondrial DNA mutations
ATP and other high-energy compounds
ATP cycle and high-energy phosphate bonds
Utilization of ATP
Other high-energy compounds
7. Lipid metabolism
Physiological functions of lipids
Energy storage and oxidation energy supply
Components of biofilm: cell membrane, organelle membrane, nuclear membrane, nerve hydrocele, etc.
Digestion and absorption of lipids
Anabolic of fat (triglycerides)
Anabolic of fatty acids
Catabolic metabolism of fat
Cholesterol metabolism
Glycerol phospholipid metabolism
Plasma lipoprotein metabolism
8. Amino acid metabolism
Physiological function and nutritional effect of protein
Physiological functions of amino acids
Synthesize proteins
Raw materials for synthesis of other substances
Convert to sugar or fat
Oxidation function
Physiological functions of proteins
The material basis of life
Participate in various life activities in the body
As energy substance oxidation supply energy
Concepts and types of essential amino acids for nutrition
9 essential amino acids for nutrition
The idiot came to the dormitory to dry his feet
Nutritional value of protein
Cereals and legumes complement each other: lysine and tryptophan
Nitrogen balance
The average nitrogen content of protein is 16%
The digestion, absorption and decay of protein in the intestine
The role of protein in digestion
Mainly digested in the small intestine
Absorption of amino acids
Decomposed by E. coli
The corruption of protein
General metabolism of amino acids
The effect of aminotransfer
The coenzyme and decarboxylase of amino acid transaminase are both pyridoxal phosphate (vitamin B6)
Deaminization
Combined deaminating (most important)
L-glutamate oxidative deylase
Non-oxidation deaminating
Metabolism of α-ketone
Thorough oxidation function
Convert to sugar and lipid compounds
Aminogenized to produce non-essential amino acids
The metabolism of ammonia
Source of ammonia
Exogenous ammonia
Absorption from the digestive tract
Endogenous ammonia
In vivo metabolism
Transport of ammonia
Must be transported to the liver or kidney in non-toxic alanine, glutamine
The way to ammonia in the body
Convert to alanine
Synthesis of glutamine
Synthesis of glutamic acid
Synthesis of urea in the liver
Ornithine cycle
Individual amino acid metabolism
Decarboxylation of amino acids
One carbon unit
source
Vector
Tetrahydrofolate FH4
significance
Metabolic disorders or FH4 deficiency can cause megalyophobic erythrocyte anemia
Methionine cycle, SAM and PAPS
Alephrine metabolism
Patients with congenital phenylalanine hydroxylase deficiency, phenypyruvateuria
Tyrosine metabolism
In the adrenal medulla and nerve tissue
In melanocytes
Transformation of amino groups
The human body lacks old tyrosinase-albinding disease
9. Nucleotide metabolism
metabolism
Raw materials for de novo synthesis of purine nucleotides and pyrimidine nucleotides
Purine: aspartic acid, glutamine, glycine, CO2, formyl
Pyrimidine: aspartic acid, glutamine, CO2
Purine nucleotide synthesis pathway and its raw materials
Pyrimidine nucleotide synthesis pathway and its raw materials
Result synthesis
Catabolic metabolism of purine nucleotides
Uric acid
Catabolic products of pyrimidine nucleotides
adjust
Major regulatory enzymes of nucleotide synthesis pathway
Biochemical mechanism of anti-nucleotide metabolic drugs
10. Transmission of genetic information
Overview
The Central Rule
DNA synthesis
Characteristics of DNA replication
Semi-reserved copy
Two-way copy
Semi-discontinuous copy
High fidelity
DNA replication system
raw material
Enzyme
template
Primers
Enzymes required for DNA replication
DNA polymerase
DNA ligase
DNA replication process of prokaryotes
DNA replication starts
DNA unstranded
Primer synthesis
Extension of DNA strands
DNA replication termination
Excision of primers
Fill in the vacancy
Connecting cutout
DNA replication process of eukaryotes
Copy start
Copy extension
Copy terminated
Reverse transcription
DNA damage and repair
DNA damage caused by ultraviolet rays mainly causes the formation of pyrimidine dimers
RNA synthesis
The composition of the transcriptional system
DNA templates
4 NTP and RNA polymerases
Certain protein factors
Necessary inorganic ions
Transcription process
Initiation of transcription
Cis-acting elements
Proximal regulatory elements
Promoter, upstream elements of promoter
Distance sequence
Enhancer
Transcription prolongation
Transcription termination
Post-transcriptional processing process
Post-transcriptional processing of mRNA
Intron
Exons
Processing of rRNA precursor
Processing of tRNA precursor
Protein biosynthesis
Protein biosynthesis system
Amino acids
mRNA
tRNA, amino acid carrier tool and adapter for protein biosynthesis
Ribosomes (nucleoproteinomes), a place for protein biosynthesis
The basic process of protein synthesis
Activation of amino acids
The beginning of peptide chain synthesis
Extension of peptide chains
Termination of peptide chain synthesis
Post-translational modification of protein
Directed delivery
Relationship between protein biosynthesis and medicine
Protein conformational disease
Human striatum spinal cord degeneration
Alzheimer's disease
Huntington's disease
Choreopathy
Gene expression regulation
Spatiotemporality of gene expression
Time specificity
Space specificity
Constitutive expression, induction and repression of genes
Multi-level regulation of gene expression
Basic elements
Basic Principles
Prokaryotic gene expression regulation
Eukaryotic gene expression regulation
Recombinant DNA technology
Common tool enzymes used in recombinant DNA technology
Restrictive endonuclease
DNA ligase
The basic principles and processes of genetic engineering
Expression of slit junction and sieve
Genetic Engineering and Medicine
11. Oncogenes and tumor suppressor genes
Growth factor
Endocrine, paracrine, autocrine
Mechanism of action
Membrane receptor
Intracellular receptors
12. Cell signaling
Signal molecules
Soluble molecular signal
Membrane tuberculosis signaling molecules require cell-to-cell contact to transmit information
Receptor
Classification
Intracellular receptors
Cell surface receptors
Functional characteristics
Highly dedicated
High affinity
Saturability
Reversibility
Specific mode of action
Membrane receptor-mediated signal transduction mechanism
G protein-coupled receptor-mediated signal transduction pathway
G protein coupled receptor
Signal to path
Protein kinase A pathway
Protein kinase C pathway
Single transmembrane receptor-mediated signal transit pathway
Single transmembrane receptor
Signal transduction path
Give an example
Intracellular receptor-mediated signal transduction mechanism
13. Biochemistry of blood and liver
Chemical composition of blood
Water and inorganic salts
Plasma protein
Non-protein nitrogen-containing substances
Nitrogen-free organic compounds
Plasma protein
Classification
Electrophoresis
Ultracentrifugation
source
Most of them are synthesized in the liver
Function
Maintain plasma colloid osmotic pressure
Maintain normal plasma pH
Transportation
Immune effects
Catalytic action
Nutritional effects
Coagulation, anticoagulation and fibrinolysis
Metabolism of red blood cells
Raw materials, sites and key enzymes for heme synthesis
Metabolic characteristics of mature red blood cells
Sugar metabolism
Lipid metabolism
Biotransformation of liver
Biotransformation reaction types and enzyme systems
Reaction type
First phase reaction
Oxidation, reduction, hydrolysis
Second phase reaction
Gluoxylic acid binding reaction
Factors influencing liver biotransformation
General influencing factors
age
gender
Nutrition
disease
Genetics
Many enzymes that induce biological transformation
Bile acid metabolism
Metabolizes by hepatocytes and secretes 300-700ml of bile every day
Chemistry of bile acids
primary
Secondary
Free type
Combination type
Raw materials for bile acid synthesis: cholesterol
Raw materials for cholesterol synthesis: acetyl-CoA
Metabolism of bile acids
primary
Secondary
Enterohepatic circulation of bile acid
Metabolic regulation of bile acids
Key enzymes for cholesterol synthesis: HMG-CoA reductase
Biliary pigment metabolism
Biliary pigments include biliverin, bilirubin, procholin and bilivine
Properties of free bilirubin and binding bilirubin
In single-nuclear phagocytosis system
In plasma
In the liver
Sub-theme
Bilirubin metabolism and jaundice
The metabolism of bilirubin in the intestine
jaundice
Hyperbilirubinemia
Hemolytic jaundice
Hepatocellular jaundice
Obstructive jaundice
Results of bile pigment metabolism tests for three types of jaundice
Red blood cells, white blood cells, platelets
The maximum absorption peak of tryptophan and tyrosine is 280nm. The maximum absorption peak of ninhydrin reaction blue-purple compound is 570nm