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Bertholf, Ph.D. Associate Professor of Pathology Chief of Clinical Chemistry & Toxicology University of Florida Health Science Center/Jacksonville  -Analytical methods used in clinical chemistryaSpectrophotometry Electrochemistry Immunochemistry Other Osmometry Chromatography Electrophoresis29)'),# !Introduction to spectrophotometryInvolves interaction of electromagnetic radiation with matter For laboratory application, typically involves radiation in the ultraviolet and visible regions of the spectrum. Absorbance of electromagnetic radiation is quantitative.ZElectromagnetic radiation !Wavelength, frequency, and energy The Electromagnetic Spectrum Visible spectrumMolecular orbital energies 'Molecular electronic energy transitions Absorption of EM radiation 4Manipulation of Beer s Law >Beer s Law error in measurement Design of spectrometric methodsThe analyte absorbs at a unique wavelength (not very common) The analyte reacts with a reagent to produce an adduct that absorbs at a unique wavelength (a chromophore) The analyte is involved in a reaction that produces a chromophoreMeasuring total proteinAll proteins are composed of 20 (or so) amino acids. There are several analytical methods for measuring proteins: Kjeldahl s method (reference) Direct photometry Folin-Ciocalteu (Lowery) method Dye-binding methods (Amido black; Coomassie Brilliant Blue; Silver) Precipitation with sulfosalicylic acid or trichloracetic acid (TCA) Biuret method.rZZrr & & + "Kjeldahl s method Direct photometryAbsorption at 200 225 nm can also be used (lmax for peptide bonds) Free Tyr and Trp, uric acid, and bilirubin interfere at 280 nm<Z+R,H/#Folin-Ciocalteu (Lowry) method$ Sometimes used in combination with biuret method 100 times more sensitive than biuret alone Typically requires some purification, due to interferences$ Biuret methodtSodium potassium tartrate is added to complex and stabilize the Cu++ (cupric) ions Iodide is added as an antioxidant$uB1 ['Measuring albuminAlbumin is the most abundant protein in serum (40-60% of total protein) Albumin is an anionic protein (pI=4.0-5.8) Enriched in Asp, Glu \ Albumin reacts with anionic dyes BCG (lmax= 628 nm), BCP (lmax= 603 nm) Binding of BCG and BCP is not specific, since other proteins have Asp and Glu residues Reading absorbance within 30 s improves specificitys#'W4V  #  W4 >g=(Specificity of bromocresol dyes u5Measuring glucose^Glucose is highly specific for b-D-Glucose The peroxidase step is subject to interferences from several endogeneous substances Uric acid in urine can produce falsely low results Potassium ferrocyanide reduces bilirubin interference About a fourth of clinical laboratories use the glucose oxidase methodNZiZGZaiGb/ . I  Ew6Glucose isomersPThe interconversion of the a and b isomers of glucose is spontaneous, but slow Mutorotase is added to glucose oxidase reagent systems to accelerate the interconversion *H; "6Measuring creatinine The reaction of creatinine and alkaline picrate was described in 1886 by Max Eduard Jaffe Many other compounds also react with picrateP  +9!Modifications of the Jaffe methodFuller s Earth (aluminum silicate, Lloyd s reagent) adsorbs creatinine to eliminate protein interference Acid blanking after color development; dissociates Janovsky complex Pre-oxidation addition of ferricyanide oxidizes bilirubin Kinetic methods456,456,> "  :Kinetic Jaffe method9Enzymatic creatinine method 7H2O2 is measured by conventional peroxidase/dye methods684!  :Enzymatic creatinine method 7H2O2 is measured by conventional peroxidase/dye methods684!  <Measuring urea (direct method)sDirect methods measure a chromagen produced directly from urea Indirect methods measure ammonia, produced from ureatZt Qz7 Measuring urea (indirect method)The second step is called the Berthelot reaction In the U.S., urea is customarily reported as  Blood Urea Nitrogen (BUN), even though . . . It is not measured in blood (it is measured in serum) Urea is measured, not nitrogen BZUZZU ? Conversion of urea/BUNA!Measuring uric acidTungsten blue absorbs at l = 650-700 nm Uricase enzyme catalyzes the same reaction, and is more specific Absorbance of uric acid at l ~ 585 nm is monitored Methods based on measurement of H2O2 are commoniZ3Z0Z:3! (D"Measuring total calciumMore than 90% of laboratories use one or the other of these methods. Specimens are acidified to release Ca++ from protein, but the CPC-Ca++ complex forms at alkaline pH@j  G#Measuring phosphatePhosphate in serum occurs in two forms: H2PO4- and HPO4-2 Only inorganic phosphate is measured by this method. Organic phosphate is primarily intracellular.(c( UI$Measuring magnesiumFormazan dye and Xylidyl blue (Magnon) are also used to complex magnesium 27Mg neutron activation is the definitive method, but atomic absorption is used as a reference method8ZJ c 6 GMeasuring iron`The specimen is acidified to release iron from transferrin and reduce Fe3+ to Fe2+ (ferrous ion)6aH/ &*Measuring bilirubiniDiazo reaction with bilirubin was first described by Erlich in 1883 Azobilirubin isomers absorb at 600 nmjZj60 +Evolution of the diazo method1916: van den Bergh and Muller discover that alcohol accelerates the reaction, and coined the terms  direct and  indirect bilirubin 1938: Jendrassik and Grof add caffeine and sodium benzoate as accelerators Presumably, the caffeine and benzoate displace un-conjugated bilirubin from albumin The Jendrassik/Grof method was later modified by Doumas, and is in common use todayvZTZTZGTStx  ,Bilirubin sub-forms HPLC analysis has demonstrated at least 4 distinct forms of bilirubin in serum: a-bilirubin is the un-conjugated form (27% of total bilirubin) b-bilirubin is mono-conjugated with glucuronic acid (24%) g-bilirubin is di-conjugated with glucuronic acid (13%) d-bilirubin is irreversibly bound to protein (37%) Only the b, g, and d fractions are soluble in water, and therefore correspond to the direct fraction a-bilirubin is solubilized by alcohols, and is present, along with all of the other sub-forms, in the indirect fractionPZZZP 4 / - (Up >  .Measuring cholesterol by L-BThe Liebermann-Burchard method is used by the CDC to establish reference materials Cholesterol esters are hydrolyzed and extracted into hexane prior to the L-B reaction,  1Enzymatic cholesterol methodsEnzymatic methods are most commonly adapted to automated chemistry analyzers The reaction is not entirely specific for cholesterol, but interferences in serum are minimalZ3Measuring HDL cholesterolUltracentrifugation is the most accurate method HDL has density 1.063  1.21 g/mL Routine methods precipitate Apo-B-100 lipoprotein with a polyanion/divalent cation Includes VLDL, IDL, Lp(a), LDL, and chylomicrons j0"S10"S1lO  4Measuring triglycerides &LDL is often estimated based on triglyceride concentration, using the Friedwald Equation: [LDL chol] = [Total chol]  [HDL chol]  [Triglyceride]/58Z:F:t     L%,Spectrophotometric methods involving enzymesOften, enzymes are used to facilitate a direct measurement (cholesterol, triglycerides) Enzymes may be used to indirectly measure the concentration of a substrate (glucose, uric acid, creatinine) Some analytical methods are designed to measure clinically important enzymes ,I b PM&Enzyme kineticsT'Enzyme kinetics\(The Michaelis-Menton equation,  _*The Michaelis-Menton curve, ])The Lineweaver-Burk plotc+Enzyme inhibition0Competitive inhibitors compete with the substrate for the enzyme active site (Km) Non-competitive inhibitors alter the ability of the enzyme to convert substrate to product (Vmax) Un-competitive inhibitors affect both the enzyme substrate complex and conversion of substrate to product (both Km and Vmax)1Z8BWd,#M-M analysis of an enzyme inhibitore-#L-B analysis of an enzyme inhibitorh.$Measuring enzyme-catalyzed reactionsThe progress of an enzyme-catalyzed reaction can be followed by measuring: The disappearance of substrate The appearance of product The conversion of a cofactor8KZVZK9j/$Measuring enzyme-catalyzed reactionsWhen the substrate is in excess, the rate of the reaction depends on the enzyme activity When the enzyme is in excess, the rate of the reaction depends on the substrate concentrationl0Enzyme cofactorso1Enzyme cofactorsp2NAD UV absorption spectraq3Enzyme reaction profilet4Measuring glucose by hexokinase The hexokinase method is used in about half of all clinical laboratories Some hexokinase methods use NADP, depending on the source of G-6-PD enzyme A reference method has been developed for glucose based on the hexokinase reactionZ> ? z  |8Measuring bicarbonateThe specimen is alkalinized to convert all forms of CO2 to HCO3-, so the method actually measures total CO2 Enzymatic methods for total CO2 are most common, followed by electrode methods6   "  0;Measuring lactate dehydrogenase Both PL and LP methods are available At physiological pH, PL reaction if favored LP reaction requires pH of 8.8-9.8 LD (sometimes designated LDH) activity will vary, depending on which method is used 'QT!;8<Measuring creatine kinase (CK) Both creatine and phosphocreatine spontaneously hydrolyze to creatinine The reverse (PCrCr) reaction is favorable, although the reagents are more expensive All methods involve measurement of ATP or ADP,ZXE.P   s=Measuring creatine kinase Potential sources of interferences include: Glutathione (Glutathione reductase also uses NADPH as a cofactor) Adenosine kinase phosphorylates ADP to ATP (fluoride ion inhibits AK activity Calcium ion may inhibit CK activity, since the enzyme is Mg++-dependent.H,ZZ,  >, )w>Measuring creatine kinase 0Since the forward (Cr PCr) reaction is slower, the method is not sensitive Luminescent methods have been developed, linking ATP to luciferin activation$,j  ?Measuring alkaline phosphatase +The natural substrate for ALKP is not known@Measuring transaminase enzymes Pyridoxyl-5-phosphate is a required cofactor Oxaloacetate and pyruvate are measured with their corresponding dehydrogenase enzymes, MD and LDZH $  &A$Measuring gamma glutamyl transferaseEMethod described by Szasz in 1969, and modified by Rosalki and Tarlow>BMeasuring amylaseHydrolysis of both a(14) and a(1 6) linkages occur, but at different rates. Hence, the amylase activity measured will depend on the selected substrate There are more approaches to measuring amylase than virtually any other common clinical analyte"ZCAmyloclastic amylase method The rate of disappearance of the blue complex is proportional to amylase activity Starch also can be measured turbidimetrically Starch-based methods for amylase measurement are not very common any morenJDSaccharogenic amylase methodNSeveral methods can be used to quantify the reducing sugars liberated from starch Somogyi described a saccharogenic amylase method, and defined the units of activity in terms of  reducing equivalents of glucose Alternatively, glucose or maltose can be measured by conventional enzymatic methods(Z(,R EChromogenic amylase method J&J Vitros application allows small dye-labeled fragments to diffuse through a filter layer Abbott FP method uses fluorescein-labeled starch,g F Defined-substrate amylase methoda-Glucosidase does not react with oligosaccharides containing more than 4 glucose residues A modification of this approach uses b-2-chloro-4-NP, which has a higher molar absorptivity than 4-NP P Q  HMeasuring lipase (direct)"The Cherry/Crandall procedure involves lipase degradation of olive oil and measurement of liberated fatty acids by titration Alternatively, the decrease in turbidity of a triglyceride emulsion can be monitored For full activity and specificity, addition of the coenzyme colipase is required,#Z , V  IMeasuring lipase (indirect)Indirect methods for lipase measurement focus on: Enzymatic phosphorylation (Glycerol kinase) and oxidation (L-a-Glycerophosphate oxidase) of glycerol, and measurement of liberated H2O2 Dye-labeled diglyceride that releases a chromophore when hydrolyzed by lipase Several non-triglyceride substrates have been proposed, as well2ZZ@Z2;EO@t< =  & 'J Post-testrFolin-Wu Jendrassik-Grof Somogyi-Nelson Kjeldahl Lieberman-Bourchard Rosalki-Tarlow Jaffe Bertholet Fisk-SubbarrowsZs       YGlucose Bilirubin Glucose/Amylase Total protein Cholesterol GGT Creatinine Urea PhosphateZZZf, .   ` ̙33` ` ff3333f` 333MMM` f` f` 3>?" dd@,|?" dd@   " @ ` n?" dd@   @@``PT    @ ` `p>> 4,(    < ?"  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'   \ <80 } 0  DProtein nitrogen fl ` ` \` I`,$D  0`B  \ 0DԔ`   \ <Ps@ ` A Total protein   \ <@Ss   QMultiply by 6.25 (100%/16%) H \ 0޽h ? ̙33D  p`(  `r ` S 0Zs  s  ` S [s <$  0 s  ` 0]s p@  <  x ` <A ??  ` <k ,$D 0 hlmax= 280 nm4 H ` 0޽h ? ̙33$   pd(  pr p S es  s  p S es<$  0 s  p <gsY IReduced form (blue)  p <msU  $Phosphotungstic/phosphomolybdic acid% %$U8  Y  p Y p <xsU y ?Protein `B p 0DԔ 'Y' p < |s 0 v (Tyr, Trp)  ,H p 0޽h ? ̙33  t*(  tr t S |s  s  t S \s <$  0 s R t s * @ x t <A ??7J  H t 0޽h ? ̙33  xP(  xr x S Ls  s  x S ,s<$  0 s H x 0޽h ? ̙33     |I (  |r | S Hs  s  | 6lsfp@f @   | <s ;Albumin XB | 0DԔ0 0 | <sz  @ BCG (pH 4.2)   | < s`Z  @ BCP (pH 5.2)   | <s|  Jgreen or purple adduct   | BsV PJ  lAbsorbance 8    | <s&  ` Time 8 l p  | p,$D  0`@ f  |f ZB  | s *Do0 f0   | <s  :30 s  |  B\ CDEXF(o0`N NhV@q0> [WjHY \ @       p pH | 0޽h ? ̙333      g (  r  S   s   S  p`<$  0  l PJ PJ,$D  0  <4sP; ` Glucose + O28   @ `J `JfB  6Do`0   64s0  Gluconic acid + H2O2V        BLs`J iGlucose oxidase l 0-6 0-,$D  0  3 BCDEFo @   <s- Peroxidase o-DianisideH   $     0s006 bOxidized o-dianiside lmax= 400 540 (pH-dependant)z2    H  0޽h ? ̙33  *(  r  S Ds  s   S s  <$  0 s R  s *pP x  <A ??`  H  0޽h ? ̙33  *(  r  S s  s   S s `<$  0 s R  s *Pp x  <A" ??<'   H  0޽h ? ̙33(  h(  ~  s *ds  s   s *sp<$  0 s H  0޽h ? ̙33  XP(  ~  s *{  {   T { Ԕ?@  B    Ns?n@`  f.Absorbance (l = 520 nm)   H\s?p  PTime (sec)    |B  T DԔ? @  Hs?L 0 90   c 0e0e    BCDE(Ff Ԕ 8c8c     ?1 d0u0@Ty2 NP'p<'pA)BCD|E|| n&;   @    ,$D  0z L@0   @0,$D  0B   T DԔ? @   HDd?0 :80 6N L@0   L@0B   T DԔ? @  H{?L0 :20 B  Z Do?@ B  Z Do?@ V  Nx{?V ,$D  0 ,Fast-reacting (pyruvate, glucose, ascorbate)(- ,,    N`{?+` ,$D  0 [Slow-reacting (protein)( z  0j   0: ,$D 0B   f DjJ?  P B   f Do?P@P   H{?@ _  TDt4   H( {? j  TDA4 h  c $A 6?? 0 W 6L  H${?` WZ ,$D  0 :creatinine (and a-keto acids)( H  0޽h ? ̙33   N(   r   S <,{`0  { R   s *` 0 `   c $A ??x     Z-{ 11ȜȜ? p <$  0 { H   0޽h ? ̙33   $*(  $r $ S p2{`0  {  $ S P3{ p <$  0 { R $ s *0 x $ <A'  ??z;   H $ 0޽h ? ̙33  0*(  r  S 8{`  {   S 9{  <$  0 { R  s * x  <A  ??V,   H  0޽h ? ̙33  z@ (   r   S  ?{  {    S @{ <$  0 { R   s *P `   c $A ??bD  H   0޽h ? ̙33,  Pl(  r  S D{  { R  s * `  c $A 9?? @pV  9H  0޽h ? ̙33  z`(  r  S R{`  {   S S{ P<$  0 { R  s *p` `  c $A ?? +% H  0޽h ? ̙33  p*(  r  S _{  {   S Z{@ `P<$  0 { R  s *  x  <A T??p  TH  0޽h ? ̙33   ^ V   (  r  S i{  {   S j{0 P<$  0 { l y q,$D  0  0t H3PO4 + (NH4)6Mo7O24 @ @y  yfB  6Do@` `  BXRyf ` \H+> c  6{   (NH4)3[PO4(MoO3)12]   <X{` ,$D  0 xlmax= 340 nmD [l p@ ,$D  0fB  6Do ``   6P{p* IMolybdenum blue    B{  @  lmax= 600-700 nmD    <|{y` <Red. H  0޽h ? ̙33  *(  r  S |{`0  {   S 0{  <$  0 { R  s *`@ x  <A V??v  VH  0޽h ? ̙33   XN(  Xr X S ̥{`0  {  X S {0 <$  0 {  X 0@{0p@  <  ` X c $A N??`%  Njl 0 ,   X ,$D 0 X <{ ,  $Fe++ lmax= 534 nmj 33`B X 0Do0 @ `B  X 0Do`0  xz 0 ,   X   ,$D 0  X <\ ,  $Fe++ lmax= 562 nmj 33`B X 0Do0 @ `B X 0Do`0  H X 0޽h ? ̙33  z(  r  S {`0  {   S {  <$  0 { R  s *0 `  c $A ??.  H  0޽h ? ̙33  P(  r  S {  {   S {p<$  0 { H  0޽h ? ̙33  P(  r  S {  {   S { <$  0 { H  0޽h ? ̙33  *(  r  S h      S  @ <$  0  R  s * p x  <A R??f/  RH  0޽h ? ̙33   D <   (  r  S       S   ` <$  0    <{`} FCholesterol esters l X  X ,$D  0  <t{p  ? Cholesterol    B s BYCDE FoYY@   <l{X` WCholesteryl ester hydroxylase ;l p p,$D  0   <{[ Pp Choles-4-en-3-one + H2O2L     B s BYCDE FoYY@9   <٨ MCholesterol oxidase }l x0  x0 ,$D 0  s BQCPDE FoQPPO@ <   Bhި\ P|  <Quinoneimine dye (lmax~500 nm)P    Bx0  [#Phenol 4-aminoantipyrine Peroxidase$ $H  0޽h ? ̙33  z (  r  S |`     S \`  <$  0  <l  0    0 ,$D  0  <w q  IHDL, IDL, LDL, VLDL `B  0Doi   <lo w 0q  .HDL + (IDL, LDL, VLDL)8   <,i Y  GDextran sulfate   < ?  ^Mg++> v  N2 11ȜȜ? ,$D  0 rNewer automated methods use a modified form of cholesterol esterase, which selectively reacts with HDL cholesterol s0 ZsH  0޽h ? ̙33  h`(  r  S >`0     S ?@ P`<$  0    <BVPP ] Triglycerides  l  p  F  ,$D  0  3 BCDE Fo@p  <H  gGlycerol + FFAs     <L pW >Lipase l ZP ZP,$D  0  BtXpVZP fGlycerophosphate + ADP    S BCDE Fo@`p   B\T  eGlycerokinase ATP Ql 0@*  0 ,$D  0  C BCDE Fo@     <0` 0 *  Dihydroxyacetone + H2O2V    <c0@  lGlycerophasphate oxidase Zl _  _ ,$D 0  3 BCDE Fo@    <g  \ Peroxidase   6  <e _  @Quinoneimine dye (lmax ~500 nm) L!   H  0޽h ? ̙33   P(  r  S t     S uP` <$  0  H  0޽h ? ̙33  7/0 (  r  S <{   68   `  0  BA W?? Wl @   @ ,$D  0  0@  >  h   c $A U??` @` U1  0$p ,$D  0 The Km (Michaelis constant) for an enzyme reaction is a measure of the affinity of substrate for the enzyme. Km is a thermodynamic quantity, and has nothing to do with the rate of the enzyme-catalyzed reaction.  g =" H  0޽h ? ̙33d   @ 0 (  r  S P   8F   Z  s *  <A X?? Xl @   @ ,$D  0  6@  >  n   s *A d??@W dH  0޽h ? ̙33y  )!P(  r  S d`     6 >  f  s *A l?? V  l  0P VP1,$D  0 MThe Lineweaver-Burk equation is of the form y = ax + b, so a plot of 1/v versus 1/[S] gives a straight line, from which Km and Vmax can be derived. ,  $  H  0޽h ? ̙33K  `$(  l @@`` @@``,$D  0  BCDE FԔ@@`  B@ `  dv B   <䯌 @a ` l [S] F l `  $` ,$D  0`2  0 00 `2  0p`2  0``2  0 p` `2   0   `2 ! 0  Z2 " s *`0Z2 # s *`0r  S ൌ   b   ByCDEpF0og&7I-gSv @ykCUC7p    y@         9,$D  0l `0  `0,$D  0`B   0D3jJ`ZB  B s *Do0   <\F0 VVmax6  l 0 @P  0 @P ,$D  0ZB  s *D3  ZB  s *D    <̽0 @P  gVmaxF $$,l P   P,$D  0`B  0D3o ZB  s *Do  <HČPp VKm8  ^l      ,$D 0Z  s *    <A o?? ~2  oH  0޽h ? ̙33H     p (  r  S ˌ   l p\  \,$D  0ZB  s *DԔp  ZB  s *DԔ    <͌ <\ x1/[S] L   BtӌK h 1/v @ l  P    ,$D  0Z2   s *PZ2   s *p`Z2   s * `Z2   s *  Z2  s *@  Z2  s * ` P B  s *Do  ,$D  0B  0Do  ,$D 0l       ,$D 0@   @    @ ZB B s *Do   <}  @  c1/Vmax @  @   0   0`B B 0ZDo p  < p0 c-1/KmB  *8  p  Z  s * p   <A j??@ e  jH  0޽h ? ̙33  P(  r  S      S |p0<$  0  H  0޽h ? ̙33  '`(  r  S      8 @ @ @@``  p,$D  0   BCDE FԔ@@`  BX@ `  dv B   <  @a ` l [S] F p   ByCDEpF0og&7I-gSv @ykCUC7p    y@          0@,$D  0& `0  @`,$D  0`B   0D3jJ`ZB  B s *Do0   <F0 VVmax6  @      `B   0D3  @ & P    ,$D  0`B  0D3o ZB  s *Do  <Pp VKm8  l  6 '6 ,$D  0  C BrC DEpF033o ZZ0KZGx D8/m0X7  ; s Q / r@          6@,$D  0fB  6D33jJ   fB  6D33jJ  @`B  0Do @   B,05 YKm(i)8 33 3333  BL 6-  A Competitive   33l  ` @ &`  @,$D  0`B !B 0Do     C BCDEpF0oi&7I3gQ`3CRyU1t*    @          .@,$D  0fB   6DjJ    " B ` eVmax(i)B   # Bd!  }  ENon-competitive  H  0޽h ? ̙33   h `   (  r  S '   $z p\  Dp ,$D