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BMB401 F00 T1-2 - A i = 4 Alkaline phmphatase catalyze the...

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Unformatted text preview: A ' . ' i = 4:: Alkaline phmphatase catalyze; the hydrolysis of p- nitro- phonylphosphate (PNP) to p-I'Litmpheno] And phosphate. . . - catalyzed roaclion. -— -. .r BMB 401 — Examination 1 -- —. . __ a; A. T11: velocity (= rate of roactimi) will be 2m if?“ R " concenumionisonztaithoftheKm. 71—" ’ ‘ Septem ber 19’ 2 000 B. The velocity will be equal to the Vmax if the E concentration is‘lfitimes the Km. _ q.- C. BOTHAaodEm‘eom-rcct. .. _.-..___ FORM 2 EDMU‘IERAnoeroorroct ., _ % _ _ During this exam you should not lie in possession or: - . . . .' / ‘ ' beeper or a cellular phnnr. Please place 1m" beeper or 5. Which one of flu:- followmg is a Mechanical catalyst? cellular phone in your book bag (alter you turn it of!!!) and A- Myoglobm place the bag against the Wall ofthe room. You can only use B. Insulin . calculators that do not have memory capabfljfi“ for Q‘hmrnbin alphabetic characters. Other calculators should also be . Collagen placed in your bag. E. Tubulm Please answer the multi le-c aice uesti m on the mm..- 5- The amino acid alanine has what R group (side chain)? sheet and mark the form it of mar test in thc FM column on the sheet. A- Hydrogen B. Amino . C. Carboxyl THESE ARE STANDARD SINGLE ANSWER 13- Amido MULTIPLE CHOICE QUESTIONS. THE POSSIBLE @flhfl ANSWERS ARE LABELED A, R. c. D AND E. SELECT Tm: SINGLE REST ANSWER AND MARK TH'E 7- The submarine upon which an enzyme acts is called APPROPRIATE CIRCLE ON THE SCANI‘RON ANSWER SHEET. (TOTAL 40 POINTS) A; Catalase Cg Substrate < 1. Enzymes can be. regulated in a rapid manner (< 1 min) by all C- Inhibitor oldie following mechanisms EXCEPT 13- 0°me E. Prosthetic group A. Substrate nil-libition B. Proteolytic cleavage 3- With 0f 011: following Statflnents about protc'm structum is C'. Induction and rcprcssion ofenzymc synthmis CORRECT? D. Phosphm‘ylation E. Produn inhibitiOn fir'fi protein consisting ofa single polypeptide chain which can him: a quatcrnary structure 2. Which ofthe following statements is TRUE? 3- The million ofSpecific disulfidc bonds directs ihe '_ folding ofa polypeptide into its tertiary structure. A. Tertiary We is stabiliZBd by covalent interactions. C- The stability ofthc quaternary structure of a protein is B: In a folded protein the hydrophilic residues are usually I'mziirti)r due to covalent bonds between sub—unis. ,- buried in tho interior ofthe protein. B Folding of globular proteins into their native um .53. 'Primary W dictates tertiary Structure. dimensional smicwre is dn'ven by the requirement for I)? The bola-pleatod sheet i5 important in the tertiary ionic interaction to occur away fiom the aqueous structure of many globular proteins. ..--.e'nV1l‘0nn1an. E. The quaint-nary structure of myoglobin is stabilized by : E- The Primary meme Ofa POIYPCPlide Chain dim”:i its ionic inmctims. L” folding into the native, three dimensional structure. 3. What two functional groups an: found in all amino acids? 9. In solution at pH 7.1, gintaminc Would possess: . amide and carbonyl I I A. Min negatiw charges and an: positive charge. _. amid: and carbonyl e B. an: tin—dissociated carboxy] gronp. 19¢an and carboxyl n rem . 0 net charge. pfmnno and carbonyl 1—"... - —Q-nfl—j . a posm've charge On Its amide group. En" amino and hydmxyI ---—-— ' ' ' ' " 5. no ionic charges. 1\ 10 WhichafthefallowmgminoacidsismeLEAST 16. Thepeptidebundhasa'backbone" ofalomsinihichofl hm ”Pb-ill“? following seqlmnces‘z . _/:3L."-C—C-N-C- '. A- ”WW EEK—c C-O—N B I)“: c. -N-C-C-C— C. aspam'c acid 9 —Cdi\l-C—N- kg)“ E- -C-N—N c- i?- - . a 17. Which of the following is NOT mpgmt in wnfjibufing 1 1. Which one of the following amino acids contains sulfur m the we an d meCI‘Lies ofm 901m. fumu'onal mflagm is capable of forming a disulfidc bond? ' '01: inc A .-crosslinjiing 3 Met“ (1 .-phospliorvlai_imi @ASPI C 901 tight winding offl'ic three collagen polvpeptidc chains Cysteine /D glvcine E Threonine E2 pmleoljnic cleavage 18. Which offlie following statements about the oxygen can—i: 12' web mm follows is a disrupt” °f ”WM“? mflobm and myogiobin is INCORRECT? 3- gimme to 1;. Myoglobin is not located 111 red blood cells . flaming B Hemoglobin is a heta-omramer. whereas mynglobin i: monomer. g- :35"? ATM quaicrnmy structure ofthe hmglobin MIMI-11131 . 3mm! -—»’ gmbflizgd by disulfide bonds _ _ _ _ D. Mel- -hcmogloblll contains ferric iron. 0 13. The novalcnt peptide bond between Hie ammo acids in a /5_" Oxygen can bind In the ferrous (reduccd form)ofjmn pro_tem Encibonc is formed by what kind afrcacuon between hem:- m boll: myuglobin and hemoglobin. - 31111110 “W33- , i9. Which of The: following statements about the reginlntim of r A. formation Ola double bond oxygen binding and release 15 INCORRECT? B mimlytic cleavage \ Ac’I/Th . . . I. . J . 6? e mused CO; levels in the tissues wants, in the D fiydmlygision (3 LA w“ [G ( (JAM ’1 _/ demasc in pH respmsible for releasing oxygen fi-om mm [291 _ _ _ _ I,.emoglobu1 match-0n d$;:lf:ao}a?::ofizu:e:$zm£c:£m ‘Imlnbg the pl—l' Increases the release of oxygen lien 31me hemoglo m. and neleasmg WW ' ’ " £11116 higher pH in the lungs cm increased binding < . . . .- oxygen to huncglnbm. 14.1nsoimimi at pI-l 7.1,Ijvsme wnqupossms _- - D. mfimiwmom fwfl-iebindinghfoxygg . . , rip hemoglobin is a reflecti 'Ul'l afits oooperativebinding @flm P054“? clw'ges 30d one “983““ m5 I/E. /1Jnder physnological milieu myogliobin has a high: C. $2113mmed W130)?! EIDUP \_/ /afilnity for oxygen dim: docs hemoglobin. ED. a pgsiljvc change cm is amide group 20. Which offlic following pmpmies would NOT be predict: - ”0 1W1"; charges for the amino acid ifiirzom'mI in a protein? . . 7‘ ' ' 15 Conszder 1h: ntlmvmg statements on secondary lat-whine. A/fi will likely be. exposed on "the mm of a folded 4/ _ _ I _ " protein. A. Ilia alpha helical structure I5 stabilized by hydrogen B. I: b has]: bonds between the elements ofthe peptide linkage. > R2251): ZBI$36|§M / B. the bet-1 PIcatedflihMLEfinIlffim‘e n3 stab-I264 by hydrogen -- E i: may be inmlvod in intraamolecular covalent /._ \ bonds between e s: c 31113 ot ammo acids. crosslniking. C / BOTH A and B are correct E. It will be found in abundance in musin‘like NElTl-[ER A Mr B are correct. glycoproleins 9" ll. Which Ul‘lhc lblluwlng Stalcmcnts 33L“; ' hemoglobin and In :nyng]<)£:;n .2; I’-.\' /. (JD/3:11 handing I0 CURREC'I' ’ A; . The hmdjng CUTVC TOr hemoglnhm shows hxpcr'u'dn: - lunches. B. The binding curve Err I'm: kjnchc-s (COOPCIaIP-‘c ox C. {Tnder physmlogmml cundllmns n'.\n,_-.ubu1 lsuniw .‘xj'gflll u-iLh greater afflmn Lhm hcmugfiuk'rl 13- Th“ binding CUn'c fiJr |‘.‘._\0|‘.;.'.Il‘l.'l <II=M$ l'lYl-Tl‘rlMl-lc kinetics. ":EI'l‘IUI Sl1\"$'S!;I-,_trnr.-|Li4l 58m burying: 5- The bLndll'Ig GfL'Infvgcr: L. t-in luvlculk I5 F<=H‘-'-"-'b'-L‘ 22. AS a catalysl. an mljnrlr. .43; LnCI'CZSCS Lhc :L:r:<nJ.|'.‘. u." Pl'xKall:\-'l l: -r|:1n‘.d “2 the Cqulllbrium ul-ihc rqeacncn _ . B. dccrcmms [he cqumbrlwn L'uu;il:'.1|[ {KER} 0: the IUflciujuL C decrease-.5 :he sundarl L'rw l'ZIC’IgV Cllwlgt‘ Ol' {lief :camjon Pr .sEows U1: allalmnrnt k'Il-quJllLl'Jl'IUJ'fl ll] ‘JJL‘ :'Eauunn /:-. dccrescs dzc cnurgv :.II‘-1<E.'ca'..'un for 131: “moron 23-.- W’mch of U16 fnilnwing I‘IIOR‘LILS |.\' NOT a fibrmu: ”mam-y A. Collagen B. Flaslin _ C“ Acsin "D- Krratln I":- Tl'you think =th “I: '1 pmtcms i1h|'-‘VC -ll'L‘ fibrous. I-‘Totcler‘. mark E, , 11 The rate of an enzx'm: c.1r.1i_\'/.<:d r5::1-.‘.rjun muybr allimud by a clung: In A Lhc tcznpcrutur: R. .va pH. C ch subsuah: cn.|-.-L'.-e;luutl.nn D Llw IUDLC mndiriuns ‘F‘.’ aEl ol'd'n: about 25. Whlch of [he lbllOWlflg ammo acids would NOT bc cxpeL-Lcd ln undtrgo post-Ulnsia-ix-nui unnilr'lcuinnz" Al’brnilm _B./5£rine (C. Asparagme D._,-isolrucme F. cyswine _/ . - . , . ZR Wlluch ol'1he fulluwlng \-'-\'JU-\. NUT l-c [‘rr-chfr-J as :l / Dorlscqutncc of 315cm? laln'n; :. 1‘ :1 _:'-1-.:lL‘|r|" A. dccrcnsL-d susccszhII.-ry k- prulrrflj. B. cnhnnccd hydrallcn pmpcr‘..:< C._ FCVLTlSlblC regulatmn ot'ar. cn. :\1J_.‘_.Rl)apc oftlxc folded prolcm ,E: 'e'xpression at Um cell surface nr as a scented pro:ej:1 '15: dcgradaunn - 1": : actwn} f. '3} For the pans. (\l'amjno fluid vai' A 'f‘hc Km IS IlLL‘. subsuam mum! v<:ix-clr1_.'e:!l_-gz.-(, :.- [ilL‘ rusmfinn. 3.11;: 3.31.135imam-:zxg-Aul: .. Is hue: r.‘ Il-lll‘. \Tl IN: :‘I.!Llf1lTL' “'-'. 'T'|.L\<i!u_m D TllL‘ EH1: LS :3 .Tj:‘.:|5'.-_'.'._ ..I -".:1lr_.- (If-11m . f' 1-: exam: E. "2'55- LLILLLs' 1f Km 11? L'. :':'- 1- " “HIE '33 Which um: .-':;.u:;w.J.-g s ;:'-. = .-:'-.tlp|'::.--helir‘ " _A. 'l'l'LL‘j.‘ arc sthiljzc-J 3.1}- :'i-:racrion5. Ll They an: Stablllzcd hj. h'uh- 46F: bonds. ‘ __ CI. The}; can. he arrmgu‘i -~I.',: --.-.:::r parallel oru'fin‘ I chums 5' J) Thcy' are. net found an r:::.-.‘: ‘ F :. r morning. I") ‘Jx'liiltil ol‘lltc follm'x'jnp I'S Lyn : physmleplml rrgulmiun .\£'-.':., - A hydl'ulysm of am- ()I' man-u Lllt‘. gin-rein :uolucuic ”A; B. cavaieln b:n..EIn-g: of :1 fit 5- gang. to mew .--_ IIJIZ:-icculc . “‘5'? __C._'c.‘1:l:1-,'_r-: :11 Total cnncm'c - = 1'). :hnngcs I.r. mir'ncclluiu E ChangesIr]Cn:1ccnlr.1‘_{(.;: -' i‘.__._'- 30 Winch of Ulc following .\'l.1§'.i.. all-05m I: :[uyzt'le\"' A. The\ an- often commune-.1 VIE/Thu} all e\'ll-‘:-1L .lv'Il3l'..'k‘l.:I: -:- . 'C'. 'J'hcy :‘rxmtm :mlJcmL-xnr. ;' i - ='.-st::1Lc binding. -. D Their QCIiv-t} may be 5:12; _: :'- filed-back irflljhifimby L'u- pnxiuct \>r':he paLhwrf-s' =n 2" i'lch they participsh :'5 They arc mlcn key rag.'.si'.|r.--_. +3145 Emmi wfy'm pathways modulated '.'-_v .‘\.-.-" --.'-'. 'nlu'bllmn. ' ~:=I=-.i3-..ns list/ad belowznclect . -..-3cl bc cxmctrd til-have me g:_;.;ll_c-;; Jim: on m;- F-r: . - - hall structure of die prawn" I the subsLiutj-m 1n n DIOIL'IE! :l .'—\ Aspm agam: m aspanic 5-.1-1 15 Alaninc L'I <<§;'j:1c (LC. TLysi'nc [:1I placr:_\ In Luna: D Argln'llk- 10 |}‘S;r>c Ti. Valuu: 1;) Isolz-uczne 32. What Isfiie mt ChBJ‘QS (overall charge or charge contributed by the side chain groups) in the following peptide at pH 7.2? -' II P 'HJN-Ala- wi‘gis Gln- Asn- Pro—Git! -N;p- lle- Tv-r-COO' (AKWQNPEDIY) £14 . . . :--| " {o D4- 1 ' .c E. +2 I I - ,1 ::f 33. The Linewcam—Burke plot is a good graphical method for determining the Km and Vmax values for an enzyme reacumi conducted in the prmce or finance of an inhibitor. Which of die following statements about this type of plot is CORRECT? w is altered in the presence ofa mpgitive unlubltot'. B/Flic initial velocity is plotted agamsi the moiprocal of / Substrate concentration. (Thesiopeafflie lineisdccreasedinthcprwenccofa W iril'iibilos. _' ' D Vmax Is altered In the prescncc of a noncommtitive inhibitor. :E/Tl'tc Km is altered in the presence of a mampetitive inhibitor. 34. Which ofd'hc following 5121mm describing cell membranes is INCORRECT? A. M are mposed ofphmpholipids which are ' mphipaihic, having hydmphilic head groups and hydrophobic tails. (B. The phospholipids form a hilayer containing proteins. " CL Trans-momma: proteins associate with membranes by ' having short alpha‘hclical domains which can interact with the lipid interior of the membrane biluyer. D. Pmins may be minted With the membrane hilayer by the pm-umslauonal addiIiOn of covalently associated /\ lipid moieties. 1- fist—translational modification with carbohydrate is '\ equired for the association of proteins with membranes. 35. Which of the following statements is NOT true for post— translalionfll nwdificalion ofproteins by phosphorylatiou‘? _flhosphoiylation is a covalent modification BPhosphorylation can activate enzymes through curdorniational changes. osphorylation frequently occurs after secretion of a ‘ rotein. /)b05phowlaliw may result in the creation of binding sitegfor specific proteins. Wren kinases may be located at the membrane, in the cytosol or in the nuclcus. D. competing for fine substrate binding 51“.. ¥ E. covalently modifying the W. 3::- 'ch ot‘the follwing is NOT a correct chipIiou of embranes? ' A. Membranes consist mainly of lipids .- oieins @holcflcrol is the major we of lipid winch makes up the membrane bilayer. C. The protein and lipid components of a mnbrme m not valentlv bound to each other. i yazmbrancs- are semi Hpenneablc 1. c. ,thej have specific pmltins which regulatc the selective cntgy of molecules and was from the extra- cellular fluid. if :Membranes have sex- oral types of functidinnl proteins, including receptms for many ligands, ptnpps for Il-Ic regulation of Ion entry and removal. and otcins which mediate u‘anSport of specific cornponen 38. Which of the following proteins DOES NO‘E'. require a post- translational modification for its function? i. _ .‘ 2‘ ’/A- myoglobin if B. nmpcptides C. zyrnogens D. mucins _ E. the SN (proto)on00gcnc tyrosine kinase 1%: i ’ 39. ich 01‘ 1h: following statements CORRE _ Y describes c aracteiistics of regulation of molecular cellular ction bv phosphm‘ylation? A; [if Phosphorylation is irreversible. § B. The kinases which add lhc phosphate: grains can also catalyze de-phosphorylation under the apgropnatc nditions. osphorylation can amphf} moon-Ling signals from [side the cell by initiation of a cascade ofintracellular .AI events which alter several palhwaya _ ’ D. iln a normal. rooting cell phosphorylation Occurs ' " fiequemly. /EI" PhosphorylatiOn of proteins can occur on the amino acid: thrconine. serine and phenylalanine. 40.'Wh.ich of the following processes frequently results I1 irreversible activation or inactivation of an enzyme? A. Phosphoq-latim l3. Feedback inhibition *Nmteolylic cloavage' if}. Association of an inhibitory suburiit E. An increas: in ionic strengfii 'n O Q N Test 1 Form 2 ' Fall 00 BMB 401 “Mm—00000 U uestion Dele¢ed ‘4 _‘ ®DQS®595‘°“‘9'“*9‘N6 _; m 0': E (Credit given for both) 26. Question Detained 27. A 28. B 29. Question DeJeted / 222 nremellggfi BMB 401 — Examination 2 October 10, 2000 FORM 2 During this exam you should not be in [remain]: of a beeper or a cellular phone. Please place your beeper, cellular phone (after ynu turn it um!) and calculator in your book bag and place the bag against the wall of the room. No calculators are needed for this cum. Please muggy the mnltiglmhoice Questions on the answer sheet and mark the form # of war test in the FM column on the sheet. THESE. ARE STANDARD SINGLE ANSWER MULTIPLE CHOICE QUESTIONS. TEE POSSIBLE ANSWERS ARE LABELED A, B. C, D AND E. SELECT THE SINGLE BEST ANSWER AND MARK THE APPROPRIATE CIRCLE ON THE SCANTRON ANSWER SHEET. (T OTAL 30 POINTS) 1. You havejust ounsmneda mml containing 100 grams of wbohydrate, 50 grams offat and 25 grams of / protein. How many calories did you consume? / _-.A-.""3'§0 H00 ( B. 660 ' @950 {_/()O p . 1250 . E. 1550 30 I 2. immediately prior to nxidative phosphowlation. all the electrons extracted fmm the oxidation ofa molecule of glucose have been collected into:- A. NADH - NADH + FADHZ NADPH _D. "EADHZ .E’ NADPH+FADH2 3 Itequal weights of the wen-I'm? W-1W*_-‘.‘?f¥ . 4 COz- fixjng enzymes suchgs pyruvate mrbfiylaseuse a menzy‘me the vitamin: i g- t. A. Pyndoxal phosphate .2;- E. Ribnflavtn .2 § C Thiarnin pymphosp. @Biotin E. Nicotinic acid 9% 3i. i 3.1 ' 5. During starvation, the b “n derives ener metabolizing: g A. Fatty acids 3:3 B. Amjnoacids l g; C. Triacylglyocrol - f @ Kctone bodies “=5 . Cholesterol 6. The most abundant ener ' exists in the form at“. reeetveinan person flyfmcogen stored at 1' and muscle B.- Muscle proteins -- ’/C/Cimtlating plasma péneius é Phospholipids' in the Ttiaqvlglyoero] m therilpose tissue 00%!) fa 7. Mmtainsouroeofthzlté‘mtemthebl \ working normal subject iii 9‘ i.‘ A. Brain ‘ _ :_‘._. B. Live: -" '-‘.- C. Kidnev " ®Mnsclc a! uring fasting, the first to be exhausted ]S (are): A. Lipopmte'tns E Ribose \ . Glycogen . Serum albumin E. Fats I- f 9. A metabolic pathway proceeds according in th: scheme R—>S->T—p_U->V~+W. A mgulatory em E, catalyzes the Eli—Faction in the pathway. Which of the following is most likcly correct for this paLhway? A. Th6 in reaction will becamlyzed by a second atory enzyme . ither metabolitr, U or V is likelyr to ix: a postive modulator, incrcasing the activity of E C. Th: first product S, is probably the primary negative modulator of E, leading to inhibition (9% 'lasl product, W, is likely to be negative . / . .uiami ofE, tcading to inhibition. E. The last product, W, is likely to bc a positive modulator, increasing I11: activity of E. 10 During vigorous exercise. mu5cles wilI incrcase secretion of: . Citrate Pl/Glucose 1 l. The net energy pmduwd (ATP) whcn fructose-6- pbosphate is convened to iantate by glycolysis is: A.l 13. The following enzymds) is (are) regulated by it phosphnrylation and dcphosphorylation: A Pyrnvatc dehydrogenase B. Giycogml phosphm‘ylase C. Pymvate kinase D. Glycogtn synthase @1 or the above 4. Which ofthe following is not a glucogem'c substance? Male acid We acid Alanine lmitic acid~ .- ' ’f:.l_’-_'.'1'l:_l . Glycerol ‘ - . FWVUOV‘J MAO—k”: Mimi? 15. Whichoneof the Krebs ml: 3 $- Qlutamic 7 . Oxaloaoetji: .‘d C. Isocitric amt}? é_. D. Malicacid j:_.- E. Suncinic ac‘fi 5-- 16. By what mec- : glycogcnolytic - in the flwr’g- ( A Afi'ectxme .. penncahiiiiy [W B Dcpmses m- ption ofDNA { 9% C Stimulatcs ~ icehzymaiiqactiviiy ’ t g} @u‘muiam ‘s orcAMri r/ E. News of the hi" 96 ,. 17. All of th: follo i-— -_ enzymes catalyze irreversible mcuons of gly 5.1- sis EXCEPr:_-§-; . Hexakinase _ c C. Phospho - . has: 1;. D. Pyrirvate [CH- '3; is 18. NADH produc-i the moplasri‘t is able to pass its electrons throu- = 'thc mitochondflal demon transport system by whic . =.".‘=' the followinginechanisms? 9‘. 71.1 _/A Specific .- “5;." rt system gables NADH to pass 2‘ gh the ochondn'al metrihrane ADPH, w ‘52: passes clectmns to cocnzyme Q {EFADH redu ._.-,. dihydmxyaqctbne phosphate to glycerolph '_ which can shuttle electrons ough the mitochondrial mmbmne . ADI-l oxidiés aspamte to oxaloanetale, Which Can enter the 'j'nitochondria 9 . 19. In glycolysis N is comma to NADH. In order for glycolysis to con _ I no, NAT.)+ may be primarily — regenerated by: K . Eu: -. - .. View a???“ T . A. e convatsioh of dihydmxyaqetonephosphate to glyceml-3—phgsphate fl ’ .' 'f ”Mi—S ’; B. the conversiogi ofqrtosalic oxaloaoaic acid to _' Ialate 3:- . . -l_ . ; 1‘ 5-311. -- e lactate defiymfizngrggglzgcuf “9’? 3 D. the oxidalivc ilecaIboxylation of malic acid E. none of the above ‘ ' j'l it [/24 VII'Mo.v-L‘_I' 5" 7 #395 E3 ._ i-ilit ;‘ {a M :J 20. Which ofthe following products and pathudys represent potenual fates for glucose-G—plmsphate in the timer“? X‘Riboee-S-phosphate via the pentase phosphate _.-; shunt pathway ,3. glucose via glumse-S-phnspbatase ”it :Biycogen via glyeose~l phosphate fatty acids via acetyl CoA of the above Whm is the primary process by which epinephrine blood Sugar? l/ ' /Sy'mhecis of carbohydrnie from fat B. Absorption ofcm‘bohydmte from the digestive mar/f); ., ._ vergiycogen breakdown . Giumneogwesis \ 22. All of the following reactions occur in muscle EXCEPT: "yuihesis of glucose from alanine " 0x1 . 'dation of ketone bodies C. Syndiexis of ATP from AD? and phosphocmatine D. oxidaiimi of lactic acid E. glycogen breakdown 23. A high insulin to glumgen ratio indiams: _ . starvation or low carbohydrate diet .- _ nutrient storage and promin embolism . mobilization (If nutrients and protein embolism D. the cfiects of severe infection E. none of the above 4. Gluconeogenesis fibm pynwate requires participation ofail oftlie fellaning enzymes EXCEPT: /"\ ”(Eff/X Pymvatc carboxylase (PC) beosphoenolpymvabe carboxykinase (PEPCK) , C. Fructose 1 6 di(bis)phosphatase ti .1‘ L’ J'rJ Glucose-G-phosphatase— 'rg fl,\:' hospbogiuoomutase 25. All of the follwing statements an . " phosphofi'uctokinase l (PFKI) are true EXCEPT: T/t is activated by fructose 2,6 his(di)ph05phate _ I' it...
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