生化复习资料(单词)
临沂人事信息-军训日记
Chapter 1 protein structure and
arginine, Arg
function
protein
biomolecular
amino acid
polarity
nonpolarity
hydrophobicity
neutrality
acidity
alkality
glycine, Gly
alanine, Ala
valine, Val
leucine, Leu
isoleucine, Ile
phenylalanine, Phe
proline, Pro
tryptophan, Trp
serine,
Ser
tyrosine, Tyr
cysteine, Cys
methionine, Met
asparagine, Asn
glutamine, Gln
threonine, Thr
aspartic
acid, Asp
glutamic acid, Glu
lysine, Lys
histidine, His
basic amino acid
acidic
amino acid
polar amino acid
neutral amino
acid
Spectrophotometry
Absorbance Spectrum
Ultraviolet
infrared
absorption peak
wavelength
solubility
side chain
aminogroup
guanidinium group
imidazolyl
carboxy group
isoelectric
point, pI
peptide
polypeptide chain
peptide bond
oligopeptide
polypeptide
amino terminal
carboxyl terminal
residue
ninhydrintriketohydrindene hydrate
imino acid
glutathione, GSH
1 12
hydrosulfide groupsulfhydryl
primary structure
secondary structure
tertiary structure
quaternary structure
α-helix
β-pleated sheet
β-turn
random coil
zinc finger
domain
peptide unit
motif
protein denature
molecular chaperone
allosteric effect
subunit
positive cooperativity
negative cooperativity
renaturation
protein coagulation
ninhydrin reaction
biuret reaction
dialysis
salt
precipitation
elctrophoresis
chromatography
prosthetic group
prion
protein
disulfide
hydrogen bond
hydrophobic interaction
electrostatic
interaction
Van der Waals interaction
Fibrous protein
Conformational change
Globular protein
Protein fold
Ionic
bond
Side chain
tetramer
dimmer
monomer
oligomer
denaturation
renaturation
Questions:
1. Can
you give an example to
elucidate the
relationship between
protein primary structure
and
function?
2. Can you give an example
to
elucidatethe protein allosteric
effect?
Chapter 2Structure and Function
of
Nucleic Acid
nucleotide
2 12
nucletic acid
deoxyribonucleic
acid, DNA
ribonucleic acid, RNA
the
chemical component
base
base pair
base pairing
ribose
phosphate
purine
adenine, A
guanine, G
pyrimidine
cytosine, C
uracil, U
thymine, T
ribose
deoxyribose
ribonucleoside
ribonucleotide
glycosidic bond
nucleoside monophosphate,
NMP
nucleoside diphosphate, NDP
nucleoside
triphosphate, NTP
phosphodiester linkage
polydoxynucleotide
polynucleotide
nitrogenous base
double helix
histone
superhelixsupercoil
positive supercoil
negative supercoil
nucleosome
RNA(small non-messenger RNAs,
snmRNAs
nucleoid
chromatin
messenger RNA,mRNA
heterogeneous nuclear RNA, hn RNA
cap
sequence
poly (A) tail
transfer RNA, tRNA
cloverleaf pattern
stem-loop
anticodon
dihydrouracil loop
ribosomal RNA, rRNA
ribosomal protein
optical density
methyl
optical density, OD
Tm, melting
temperature
annealing
heteroduplex
renaturation
Nuclease
deoxyribonuclease, DNase
ribonuclease,
RNase
ribozyme
3 12
DNAzyme
restriction endonuclease
exonuclease
gram molecule
base stacking
amino acid
arm
groove
right-handed DNA
left-
handed double helix
cruciform
chromosome
intrastrand hydrogen bonding
acceptor stem
D loop
anticodon loop
oligonucleotide
base complementrity
hyperchromatic effect
ribozyme
stability
Questions:
1. The main classification of RNA in
cell,
and elucidate their function,
respectively?
2. Elucidate the different between
DNA and
RNA?
3. What is hyperchromatic effect?
4 12
Chapter 3 Enzyme
enzyme
biocatalyst
apoenzyme
cofactor
simple enzyme
conjugated enzyme
metalloenzyme
metal-activated enzyme
coenzyme
prosthetic group
monomeric
enzyme
oligomeric enzyme
multienzyme
system
multifunctional enzyme
tandem
enzyme
holoenzyme
essential group
active center
active site
binding
group
catalytic group
activation energy
specificity
absolute specificity
relative specificity
stereo specificity
induced-fit hypothesis
proximity effect
orientation arrange
Kinetic
Michaelis-menten equation
Vmax, maximum
velocity
Ｋm, Michaelis constant
turnover
number
double reciprocal plot
Lineweaver-
Burk
optimum temperature
optimum pH
inhibitor
irreversible inhibition
reversible inhibition
competitive
inhibition
non-competitive inhibition
uncompetitive inhibition
activator
essential activator
non-essential
activator
regulation
zymogen
allosteric regulation
allosteric enzyme
allosteric site
allosteric effector
covalent modification
induction
repression
isoenzyme
oxidoreductases
transferases
hydrolases
lyases
isomerases
ligases, synthetases
enzyme
coupled assays
immobilized enzyme
abzyme
substrate
catalytic power
reaction
catalyzed rate
velocity
unimolecular
reaction
biomolecular reaction
second-
order
first-order
free energy of
activation
polymerase chain reaction
reversibly
association
dissociation
assumption
bind
equilibrium
constant
direction
concentration
horizontal coordinate
vertical coordinate
5 12
graphical pattern
interpretation
affinity
lactate
dehydrogenase, LDH
covalent modification
glycogen phosphorylase
ligase
initial
velocity
Q
1. List six general ways
in which
enzyme activity is controlled?
2.
What is enzyme? And elucidate its
specificity?
starch
glycogen
cellulose
glycolipid
glycoprotein
glucose
transporter
glycolysis
glycolytic pathway
pyruvate
lactate
hexokinase
glucose-6-phosphate, G-6-P
glucokinase
fructose-6-phosphate, F-6-P
6-phosphfructokinase-1
Chapter 4
Metabolism of
aldolase
phosphotriose
isomerase
glyceraldehyde-3-phosphate
dehydrogenase
phosphoglycerate kinase
substrate level phosphorylation
phosphoglycerate mutase
enolase
phosphoenolpyruvate, PEP
pyruvate kinase
protein kinase, PK
Aerobic Oxidation of
Carbohydrate
acetyl CoA
Tricarboxylic acid
Cycle, TAC
oxaloacetic acid
6 12
Carbohydrates
carbohydrates
monosacchride
oligosaccharide
polysaccharide
glycoconjugate
glucose
fructose
galactose
ribose
maltose
sucrose
lactose
citric acid
carboxy group carboxyl
dehydrogenation
decarboxylation
citrogenasecondensing
enzyme
α-ketoglutarte dehydrogenase complex
isocitrate dehydrogenase
pyruvate
dehydrogenase
dihydrolipoyltransacetylate
dihydrolipoamide dehydrogenase
α-ketoglutarate
succinyl CoA
fatty
acid
porphyrin
malic acid apple acid
malic enzyme
oxaloacetic decarboxylase
citrate cleavage enzyme
pyruvate
carboxylase
aepfelsaure-dehydrogenase
glutamic-oxal(o)acetic transaminase,
GOTaspartate aminotransferase
respiratory
chain
key enzyme
oxidative phosphorylation
adeynlate kinase;AK
Pastuer effect
Pentose Phosphate Pathway
3-phosphoglyceraldehyde,
G3Pglyceraldehyde
3-phosphate
7 12
fructose-6-phosphate;lactacidogen
cell
sap;cytochyma
stage; phase
G6PD
hydrogen
ribose phosphate;ribose
phosphoric
acid;RP
pentose phosphate shunt
G6P;glucose 6-phosphate
ketone group
aldehyde group
transfer reaction
hydrogen donor
biosynthesis;biosynthesize
bioconversionbiological
transformation
reducibility
Glycogenesis and
Glycogenolysis
glycogen
glucosidic
bond;glycosidic bond
glycogenesis
glucophosphomutaseglycophosphomu
tase
hemiacetal
phosphate group
uridine
diphosphate glucose , UDPG
glycogen synthase
pyrophosphorylase
glycogenolysis
phosphorylase
lactic acid cycle
glucuronate;glucuronic acid
glycogen
phosphorylase
covalent modification
cascade amplification
glucagon
epinephrine
dephosphorylation
glycogen
storage diseases
Gluconeogenesis
gluconeogenic pathway
pyruvate carboxylase
substratecycle
futile cycle
blood
glucose
acid-base equilibrium
lactose
cycle
insulin
oxidation
glucose
tolerence
glucose tolerance test, GTT
hyperglycemia
glucosuria
renal glucose
threshold
diabetes mellitus, DM
hypoglycemia
hypoglycemic shock
Q
1. Explain pentose phosphate
8 12
pathway and elucidate the
signification?
2. Elucidate the function of
oxaloacetic
acid in metabolism of
carbohydrates.
Chapter 5Metabolism of Lipid
lipid
triacylglycerols,TAG
triglyceride, TG
fat
lipoid
cholesterol, CHOL
cholesterol ester, CE
phospholipid, PL
sphingolipids
phosphoglycerides
unsaturated fatty acids
digestion
absorption
micelles
colipase
mixed micelles
chylomicron,
CM
apolipoprotein
monoglyceride
DG;diacylglycerol
hormone-sensitive
triglyceride lipase ,
HSL
lipolytic
hormones
acyl-CoA synthetase
ketone body,
acetone body
activation
energy-rich
phosphate bond
hexadecanoic acid
hydration
thiolysis
peroxisome
propanoic acid
carboxylase
racemase
mutase
acetoacetate
β-hydroxybutyrate
acetone
hydroxybutyric acid
overeating
starvation
malonyl CoA
acyl-CoA
carnitine acyl transferase
palmitic acid
citrate pyruvate cycle
acetyl CoA
carboxylase
rate-limiting enzyme
biotin
Escherichia coli
fatty acyl group
thioesterase
acyl carrier protein, ACP
phosphopan tetheinethioethylamine
Prostaglandin, PG
thromboxane, TX
leukotrienes, LT
5-HPETE,
5-hydroperoxy-eicotetraenoic acid
Phospholipid
glycerol phosphatide
phosphatidyl inositol
cephalin
phosphatidyl serine
lecithin
cardiolipin
phospholipid exchange proteins
phospholipase , PLA
sphingosine
Cholesterol
cortisol, hydrocortisone
bile acid
lipoprotein
chylomicron, CM
very low density lipoprotein, VLDL
low
density lipoprotein, LDL
high density
lipoprotein, HDL
apolipoprotein, apo
chylomicron
lipoprotein lipaseLPL
very
low density lipoprotein, VLDL
low density
lipoprotein, LDL
9 12
scavenger
receptor, SR
high density lipoprotein, HDL
reverse cholesterol transport, RCT
ATP-
binding cassetle transporter A1
cholesterol-
efflux regulatory protein,
CERP
motif
hyperlipoproteinemia
hereditary defect
choline
heparin
LDL receptor
Chylomicron
Q
1. What is
apolipoprotein and the
main function?
2.
what is the classification of lipase
and their
function?
3. Elucidate the functions and
iron-sulfur protein
cytochrome
oxidative phosphorylation
substrate level
phosphorylation
chemiosmotic hypothesis
uncoupling agents
oligomycin
respiratory control ratio, RCR
mitochondrion, mitochondria(复)
creatine
kinase
phosphocreatine
transporter
permeability
α-glycerophosphate shuttle
malate-asparate shuttle
adenine
nucleotide transporter
transmembrane
transport
catalase
perioxidase
superoxide dismutase
monoxygenase
mixed-function oxidase
hydroxylase
solubility
hydrogen donor
PO ratio
oligomycin sensitivity conferring
characteristic of triglyeride in
energy
metabolism?
Chapter6 Biological
Oxidation
respiratory chain
electron
transfer chain
complex
ubiquinone
10
12
protein, OSCP
Q
1. How
to understand that the ATP is
the center of
energy metabolism?
2. What is hydrogen donor
and
electron donor?
3. What is oxidative
phosphorylation?
And try to elucidate the
γ-glutamyl cycle
putrefaction
amines
false neurotransmitter
ammonia
half-
life
protein turnover
cathepsin
ubiquitin
ubiquitination
proteasome
metabolic pool
transamination
transaminase
urea
blood ammonia
alanine-glucose cycle
ornithine cycle
urea cycle
Krebs- Henseleit cycle
carbamoyl phosphate synthetaseⅠ,
CPS-Ⅰ
citrulline
ornithine carbamoyl
transferase,OCT
energy-rich phosphate bond
hyperammonemia
ammonia poisoning
decarboxylation
γ-aminobutyric acid, GABA
taurine
11 12
mechanism?
Chapter 7 Metabolism of Amino
Acids
nitrogen balance
essential amino acid
nutrition value
complementation
digestion
absorption
putrefaction
pepsinogen
pepsin
endopeptidase
exopeptidase
oligopeptidase
enterokinase
trypsin
exopeptidase
carboxypeptidase
elastase
aminopeptidase
dipeptidase
histamine
vasodilator
5-hydroxytryptamine, 5-HT
polyamines
one carbon unit
methyl
methylene
methenyl
formyl
formimino
tetrahydrofolic acid, THFA,FH
4
methionine cycle
creatinine
sulfate;sulphate
catecholamine
melanin
phenyl keronuria, PKU
branched chain amino
acid
nitricoxide synthase;NOS
Q
1. What is ornithine cycle? Elucidate
the
process and
physiological
functions.
2.
Elucidate the
pathway of amino
acids metabolism?
3.
Elucidate the
pathway of synthesis
of urea?
Chapter
Nucleotides
nucleoside
8Metabolism of
12 12
Chapter 1 protein structure and
arginine, Arg
function
protein
biomolecular
amino acid
polarity
nonpolarity
hydrophobicity
neutrality
acidity
alkality
glycine, Gly
alanine, Ala
valine, Val
leucine, Leu
isoleucine, Ile
phenylalanine, Phe
proline, Pro
tryptophan, Trp
serine,
Ser
tyrosine, Tyr
cysteine, Cys
methionine, Met
asparagine, Asn
glutamine, Gln
threonine, Thr
aspartic
acid, Asp
glutamic acid, Glu
lysine, Lys
histidine, His
basic amino acid
acidic
amino acid
polar amino acid
neutral amino
acid
Spectrophotometry
Absorbance Spectrum
Ultraviolet
infrared
absorption peak
wavelength
solubility
side chain
aminogroup
guanidinium group
imidazolyl
carboxy group
isoelectric
point, pI
peptide
polypeptide chain
peptide bond
oligopeptide
polypeptide
amino terminal
carboxyl terminal
residue
ninhydrintriketohydrindene hydrate
imino acid
glutathione, GSH
1 12
hydrosulfide groupsulfhydryl
primary structure
secondary structure
tertiary structure
quaternary structure
α-helix
β-pleated sheet
β-turn
random coil
zinc finger
domain
peptide unit
motif
protein denature
molecular chaperone
allosteric effect
subunit
positive cooperativity
negative cooperativity
renaturation
protein coagulation
ninhydrin reaction
biuret reaction
dialysis
salt
precipitation
elctrophoresis
chromatography
prosthetic group
prion
protein
disulfide
hydrogen bond
hydrophobic interaction
electrostatic
interaction
Van der Waals interaction
Fibrous protein
Conformational change
Globular protein
Protein fold
Ionic
bond
Side chain
tetramer
dimmer
monomer
oligomer
denaturation
renaturation
Questions:
1. Can
you give an example to
elucidate the
relationship between
protein primary structure
and
function?
2. Can you give an example
to
elucidatethe protein allosteric
effect?
Chapter 2Structure and Function
of
Nucleic Acid
nucleotide
2 12
nucletic acid
deoxyribonucleic
acid, DNA
ribonucleic acid, RNA
the
chemical component
base
base pair
base pairing
ribose
phosphate
purine
adenine, A
guanine, G
pyrimidine
cytosine, C
uracil, U
thymine, T
ribose
deoxyribose
ribonucleoside
ribonucleotide
glycosidic bond
nucleoside monophosphate,
NMP
nucleoside diphosphate, NDP
nucleoside
triphosphate, NTP
phosphodiester linkage
polydoxynucleotide
polynucleotide
nitrogenous base
double helix
histone
superhelixsupercoil
positive supercoil
negative supercoil
nucleosome
RNA(small non-messenger RNAs,
snmRNAs
nucleoid
chromatin
messenger RNA,mRNA
heterogeneous nuclear RNA, hn RNA
cap
sequence
poly (A) tail
transfer RNA, tRNA
cloverleaf pattern
stem-loop
anticodon
dihydrouracil loop
ribosomal RNA, rRNA
ribosomal protein
optical density
methyl
optical density, OD
Tm, melting
temperature
annealing
heteroduplex
renaturation
Nuclease
deoxyribonuclease, DNase
ribonuclease,
RNase
ribozyme
3 12
DNAzyme
restriction endonuclease
exonuclease
gram molecule
base stacking
amino acid
arm
groove
right-handed DNA
left-
handed double helix
cruciform
chromosome
intrastrand hydrogen bonding
acceptor stem
D loop
anticodon loop
oligonucleotide
base complementrity
hyperchromatic effect
ribozyme
stability
Questions:
1. The main classification of RNA in
cell,
and elucidate their function,
respectively?
2. Elucidate the different between
DNA and
RNA?
3. What is hyperchromatic effect?
4 12
Chapter 3 Enzyme
enzyme
biocatalyst
apoenzyme
cofactor
simple enzyme
conjugated enzyme
metalloenzyme
metal-activated enzyme
coenzyme
prosthetic group
monomeric
enzyme
oligomeric enzyme
multienzyme
system
multifunctional enzyme
tandem
enzyme
holoenzyme
essential group
active center
active site
binding
group
catalytic group
activation energy
specificity
absolute specificity
relative specificity
stereo specificity
induced-fit hypothesis
proximity effect
orientation arrange
Kinetic
Michaelis-menten equation
Vmax, maximum
velocity
Ｋm, Michaelis constant
turnover
number
double reciprocal plot
Lineweaver-
Burk
optimum temperature
optimum pH
inhibitor
irreversible inhibition
reversible inhibition
competitive
inhibition
non-competitive inhibition
uncompetitive inhibition
activator
essential activator
non-essential
activator
regulation
zymogen
allosteric regulation
allosteric enzyme
allosteric site
allosteric effector
covalent modification
induction
repression
isoenzyme
oxidoreductases
transferases
hydrolases
lyases
isomerases
ligases, synthetases
enzyme
coupled assays
immobilized enzyme
abzyme
substrate
catalytic power
reaction
catalyzed rate
velocity
unimolecular
reaction
biomolecular reaction
second-
order
first-order
free energy of
activation
polymerase chain reaction
reversibly
association
dissociation
assumption
bind
equilibrium
constant
direction
concentration
horizontal coordinate
vertical coordinate
5 12
graphical pattern
interpretation
affinity
lactate
dehydrogenase, LDH
covalent modification
glycogen phosphorylase
ligase
initial
velocity
Q
1. List six general ways
in which
enzyme activity is controlled?
2.
What is enzyme? And elucidate its
specificity?
starch
glycogen
cellulose
glycolipid
glycoprotein
glucose
transporter
glycolysis
glycolytic pathway
pyruvate
lactate
hexokinase
glucose-6-phosphate, G-6-P
glucokinase
fructose-6-phosphate, F-6-P
6-phosphfructokinase-1
Chapter 4
Metabolism of
aldolase
phosphotriose
isomerase
glyceraldehyde-3-phosphate
dehydrogenase
phosphoglycerate kinase
substrate level phosphorylation
phosphoglycerate mutase
enolase
phosphoenolpyruvate, PEP
pyruvate kinase
protein kinase, PK
Aerobic Oxidation of
Carbohydrate
acetyl CoA
Tricarboxylic acid
Cycle, TAC
oxaloacetic acid
6 12
Carbohydrates
carbohydrates
monosacchride
oligosaccharide
polysaccharide
glycoconjugate
glucose
fructose
galactose
ribose
maltose
sucrose
lactose
citric acid
carboxy group carboxyl
dehydrogenation
decarboxylation
citrogenasecondensing
enzyme
α-ketoglutarte dehydrogenase complex
isocitrate dehydrogenase
pyruvate
dehydrogenase
dihydrolipoyltransacetylate
dihydrolipoamide dehydrogenase
α-ketoglutarate
succinyl CoA
fatty
acid
porphyrin
malic acid apple acid
malic enzyme
oxaloacetic decarboxylase
citrate cleavage enzyme
pyruvate
carboxylase
aepfelsaure-dehydrogenase
glutamic-oxal(o)acetic transaminase,
GOTaspartate aminotransferase
respiratory
chain
key enzyme
oxidative phosphorylation
adeynlate kinase;AK
Pastuer effect
Pentose Phosphate Pathway
3-phosphoglyceraldehyde,
G3Pglyceraldehyde
3-phosphate
7 12
fructose-6-phosphate;lactacidogen
cell
sap;cytochyma
stage; phase
G6PD
hydrogen
ribose phosphate;ribose
phosphoric
acid;RP
pentose phosphate shunt
G6P;glucose 6-phosphate
ketone group
aldehyde group
transfer reaction
hydrogen donor
biosynthesis;biosynthesize
bioconversionbiological
transformation
reducibility
Glycogenesis and
Glycogenolysis
glycogen
glucosidic
bond;glycosidic bond
glycogenesis
glucophosphomutaseglycophosphomu
tase
hemiacetal
phosphate group
uridine
diphosphate glucose , UDPG
glycogen synthase
pyrophosphorylase
glycogenolysis
phosphorylase
lactic acid cycle
glucuronate;glucuronic acid
glycogen
phosphorylase
covalent modification
cascade amplification
glucagon
epinephrine
dephosphorylation
glycogen
storage diseases
Gluconeogenesis
gluconeogenic pathway
pyruvate carboxylase
substratecycle
futile cycle
blood
glucose
acid-base equilibrium
lactose
cycle
insulin
oxidation
glucose
tolerence
glucose tolerance test, GTT
hyperglycemia
glucosuria
renal glucose
threshold
diabetes mellitus, DM
hypoglycemia
hypoglycemic shock
Q
1. Explain pentose phosphate
8 12
pathway and elucidate the
signification?
2. Elucidate the function of
oxaloacetic
acid in metabolism of
carbohydrates.
Chapter 5Metabolism of Lipid
lipid
triacylglycerols,TAG
triglyceride, TG
fat
lipoid
cholesterol, CHOL
cholesterol ester, CE
phospholipid, PL
sphingolipids
phosphoglycerides
unsaturated fatty acids
digestion
absorption
micelles
colipase
mixed micelles
chylomicron,
CM
apolipoprotein
monoglyceride
DG;diacylglycerol
hormone-sensitive
triglyceride lipase ,
HSL
lipolytic
hormones
acyl-CoA synthetase
ketone body,
acetone body
activation
energy-rich
phosphate bond
hexadecanoic acid
hydration
thiolysis
peroxisome
propanoic acid
carboxylase
racemase
mutase
acetoacetate
β-hydroxybutyrate
acetone
hydroxybutyric acid
overeating
starvation
malonyl CoA
acyl-CoA
carnitine acyl transferase
palmitic acid
citrate pyruvate cycle
acetyl CoA
carboxylase
rate-limiting enzyme
biotin
Escherichia coli
fatty acyl group
thioesterase
acyl carrier protein, ACP
phosphopan tetheinethioethylamine
Prostaglandin, PG
thromboxane, TX
leukotrienes, LT
5-HPETE,
5-hydroperoxy-eicotetraenoic acid
Phospholipid
glycerol phosphatide
phosphatidyl inositol
cephalin
phosphatidyl serine
lecithin
cardiolipin
phospholipid exchange proteins
phospholipase , PLA
sphingosine
Cholesterol
cortisol, hydrocortisone
bile acid
lipoprotein
chylomicron, CM
very low density lipoprotein, VLDL
low
density lipoprotein, LDL
high density
lipoprotein, HDL
apolipoprotein, apo
chylomicron
lipoprotein lipaseLPL
very
low density lipoprotein, VLDL
low density
lipoprotein, LDL
9 12
scavenger
receptor, SR
high density lipoprotein, HDL
reverse cholesterol transport, RCT
ATP-
binding cassetle transporter A1
cholesterol-
efflux regulatory protein,
CERP
motif
hyperlipoproteinemia
hereditary defect
choline
heparin
LDL receptor
Chylomicron
Q
1. What is
apolipoprotein and the
main function?
2.
what is the classification of lipase
and their
function?
3. Elucidate the functions and
iron-sulfur protein
cytochrome
oxidative phosphorylation
substrate level
phosphorylation
chemiosmotic hypothesis
uncoupling agents
oligomycin
respiratory control ratio, RCR
mitochondrion, mitochondria(复)
creatine
kinase
phosphocreatine
transporter
permeability
α-glycerophosphate shuttle
malate-asparate shuttle
adenine
nucleotide transporter
transmembrane
transport
catalase
perioxidase
superoxide dismutase
monoxygenase
mixed-function oxidase
hydroxylase
solubility
hydrogen donor
PO ratio
oligomycin sensitivity conferring
characteristic of triglyeride in
energy
metabolism?
Chapter6 Biological
Oxidation
respiratory chain
electron
transfer chain
complex
ubiquinone
10
12
protein, OSCP
Q
1. How
to understand that the ATP is
the center of
energy metabolism?
2. What is hydrogen donor
and
electron donor?
3. What is oxidative
phosphorylation?
And try to elucidate the
γ-glutamyl cycle
putrefaction
amines
false neurotransmitter
ammonia
half-
life
protein turnover
cathepsin
ubiquitin
ubiquitination
proteasome
metabolic pool
transamination
transaminase
urea
blood ammonia
alanine-glucose cycle
ornithine cycle
urea cycle
Krebs- Henseleit cycle
carbamoyl phosphate synthetaseⅠ,
CPS-Ⅰ
citrulline
ornithine carbamoyl
transferase,OCT
energy-rich phosphate bond
hyperammonemia
ammonia poisoning
decarboxylation
γ-aminobutyric acid, GABA
taurine
11 12
mechanism?
Chapter 7 Metabolism of Amino
Acids
nitrogen balance
essential amino acid
nutrition value
complementation
digestion
absorption
putrefaction
pepsinogen
pepsin
endopeptidase
exopeptidase
oligopeptidase
enterokinase
trypsin
exopeptidase
carboxypeptidase
elastase
aminopeptidase
dipeptidase
histamine
vasodilator
5-hydroxytryptamine, 5-HT
polyamines
one carbon unit
methyl
methylene
methenyl
formyl
formimino
tetrahydrofolic acid, THFA,FH
4
methionine cycle
creatinine
sulfate;sulphate
catecholamine
melanin
phenyl keronuria, PKU
branched chain amino
acid
nitricoxide synthase;NOS
Q
1. What is ornithine cycle? Elucidate
the
process and
physiological
functions.
2.
Elucidate the
pathway of amino
acids metabolism?
3.
Elucidate the
pathway of synthesis
of urea?
Chapter
Nucleotides
nucleoside
8Metabolism of
12 12