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生化名词解释

作者:高考题库网
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2021-02-12 23:33
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2021年2月12日发(作者:球团)


生化名词解释



1.



Isoelectrrc point (PI):


AAs in solution at certaon PH are predominately in dipolary fom,fully ionized but without net charge due


to-COO and-NH3+groups.



2.



Primary structure of protein:


A linear connection of AAS along the protein chain,which is linked together by is also called


amino sequence.



3.



Secondary structure of protein:


A local spatial structure of a certain



peptides segment,that is, the relatice position of backbone atoms of


this peptide segment.



4.



Motift:


When several local peptides of defined secondary structures are close enough space,they are able to form


a Particularsular super-secondary structure.


Forexample



Zincfinger,HLH(helix-loop- helix),HTH(helix-turn-helix),Leucine zipper.



5.



Pertiary structure:


The spatial positions of all atoms of a protein, i..e,thethree-dimensional(3D) arrangement of all atoms.



6.



Auaternary structure:


The spatial arrangement of multiple subunits of a protein.



7.



Domain:



large polypeptides may be organized into structurally close but functionally independentunits.



8.



Denaturation:


A process in which a protein loses its native conformation under the treatment of denaturants..(DEcreaes



in solubility;incresse the visecosity;lose the biological activity;losecrystalizability;be susceptible to enzymatic


digestion).



9.



Hybridization:


TwoDNAs


form


different


spacies


are


completely


denatured


by



mixedand


slowly


mentary DNA strands of each species will associste and anneal to form normal the


different


dans


have


significance


homology,the


will


teed


to


form


partiarl


duplexes


or


hybrids


with


cach


other,this is called hybridization.



10.



Denaturation of DNA:


The unfolding of the duplex strsnds into signle chains is referred to asdenaturation.






1


11.



Meltion temperature(TM):


A260The



temperature at which UV adsorption reaches the half of the maximum value as=lsomens that


about 50




of the dsDNA is disassociated into the single-stranded DNA.




12.



Enzymes:


A biomolecule. Either protion or nucleic acid, that catalyzes aspecific chemical reaction.


They have extraordinary catalytic power and ahigh degree of spaecifity for their substrates.



13.



Active centers:


Some


functional


groups


are


close


enough


in


sasce


to


form


a


hydrophobic


portion


where


substrates


are


catalyzed into products within the confines of a pocket on the enzyme.



14.



Isoenzyme:


A group of enzymes that catalyze the same reaction but differ form each other in their structure,substrate


affinity, V max, and/of regulatory properties.



15.



Km:



The


substrate


concentrates


at


which


enzyme- catalyzed


reaction


proceeds


at


one-half


itsmaximum


velocity.



16.



Ribozymes:


Ribonucleic acid(RNA) molecules with catalytic; RNA enzymes.



17.



Glycolysis:


A molecule of glucose is degraded in a series of enzymatic reaction to yield two molecules of or lactate in



cyto


sol. glucoss(G)→lactic acid (lactic acid(lack of O2)




18




Gluconeogenesis:


The process of transformation of non-carbohydrates to glucose or glycogen.



18.



TCA:


The


reaction


procedure


is


a


cycle;form


acetyl


CoA+oxaloacetic


acid→citric


acid


on,by


a


few


times


of


dehydrogenesis and decarboxylation→oxaloacetic acid cycle;Also called citrate/Krebs cycle.




19.



Cori cycle:


A


metabolic


process


in


which


lactate,produced


in


tissues


such


as


muscle,is


transferred


to


liver


where


it


becomes a substrate in gluconeogenesis.(prevent acidosis;reduced lactate).



20.



AEerobic oxidation of glucose:


The process of complete oxidation of glucose to CO2 and water with liberation of energy as The form of


e(G)


→H2O+CO2(O2)




21.



Biological oxidization:


the process in which substance(Carbohydrate,lipid,AAs)are oxidized in living organism.



2


22.



Respiratory china(Electron transfer chain,ETC):


A chain in the inner membrara of the mitochondria consists of redox carriers for transferring electrons


form the substrate to molecular an oxygen ion,which combines with protons to form water.



23.



P/O ration:


is the number of inorganic phosphates incorporates into ATP per oxyfen atom consumed.(Number of mol of


ATP/2H)



25.



Hormone sensitive lipase (HSL):


TG


lipase


is


the


rate-limiting


enzyme


in


the


TG


degradation


in


adipose



is


alsonamed


HSL


because it is regulated some hormones.



26.



Oxidative phosphorylation:


The


enzymatic


phosphorylation


of


ADP


to


ADP


coupled


to


clectron


transfer


from


a


substrate


from


a


substrate to molecular oxygen.



27.



Substrate level phosphorylation:



phosphorylation


of


ADP


or


some


other


nucleoside


5'-diphosphate


coupled


to


the


dehydrogenation


of


an


organic substrate; independent of the electron



transfer chain.



28.



Putrefaction of protein:



some un- digested proteins and no absorbed are anaerobic by the bacteria in intestine. The products are toxic


to body except few viamin and fatty acid.



29.



Essential fatty acids (EFA):


Liinoleic, Linolenic and arechidonic acids are called essential fatty acids,because they cannot be synthesized


by the body and must be obtained through diet.



30.




Fat mobilization:



The triacyglycerol stored in the adipocytes are hydrolysized by lipsses,to produce free fatty acids(FFA) and


glycerol, which are released to the blood, this process is called fat mobilization.




31.




Ketone bodies:



water-soluble fuels normally exported by the liver but overproduced during fasting or in underated diabetes


mellitus, including acetoactate,


β


-hydroxybutyrate,and acetone.



32.



Essential amino acids:



acids that can not be synthesized by the body and must be obtained from the diet. 8 kinds of essential AAs:


Val,Ile,LEU,Phe,Met,Trp,Thr,Lys.



33.



Union deamination:



The


α


-amino group of most amino acids is transfereed to


α


-ketoglutarate toform a


α


-keto acid and glutamate


by


transaminase,Glutamate


is


then


oxidatively


deaminated


to


yied


ammonia


and


α


-ketoglutarate


by


glutamate dehydrogenase.



3

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