Acid phosphatase AcP

Sample material Acidified serum, acidified EDTA plasma or acidified heparin plasma. 

Drug or metabolite in sample Concentration up to which no interference occurred [mg/1] Concentration usually appearing in serum [mg/l] Interference, direction [mg/1] Clinically relevant 

Acetoacetic acid,p-aminosalicylic acid, gentisic acid, pansporin, and bilirubin react with diazo dye Fast Red TR Salt. The addition of sodium tartrate to a final concentration of 0.05 mol/1 (pH S.S.) inhibits the prostatic isoenzyme of acid phosphatase and permits the measurement of the result due primarily to these interferents. AcP in samples suspected to contain these interferents may be analyzed before and after treatment with sodium tartrate to get the AcP and Blank results, respectively. 

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What is the cause of elevation in serum acid phosphatase (ACP) activity in Gaucher disease ... 

The acid phosphatase (ACP) method, developed by Bellavite et al. [151], is based on acid phosphatase platelet activity. Acid phosphatase is a stable enzyme present in platelets. This method is similar to the LDH method. It uses regular PRP and the same Triton-X to completely lyse attached platelets. But in this test, a different enzyme (acid phosphatase) is measnred. On addition of p-nitrophenyl phosphate snbstrate, acid phosphatase converts the snbstrate into p-nitrophenol, which can be easily measnred by a photospectrometer at a wavelength of 405 nm. Side-by-side comparison of both DCH and ACP assays snggests that the ACP assay is better than the LDH assay in terms of reproducibility [152]. 

Prostate carcinoma Acid phosphatase (ACP) Prostate specific antigen (PSA)... 

The effects of organic molecules and phosphate on the adsorption of acid phosphatase on various minerals, and kaolinite in particular, have been investigated by Huang et al. [97]. The Langmuir affinity constant for AcP adsorption by kaolinite follows the series tartrate (K — 97.8) > phosphate (K= 48.6) > oxalate (K — 35.6) > acetate (K= 13.4). At low concentration, acetate even promoted the adsorption of acid phosphatase. It was considered that competitive interactions between anionic adsorbates can occur directly through competition for surface sites and indirectly through effects of anion adsorption on the surface charge and protonation. 

Fig. 12. Diagram of elution pattern of red cell acid phosphatase and various markers on Biogel P 60. The position of the various protein markers was determined both by optical density determination and by starch gel electrophoresis of the individual fractions (83). The experiment was carried out using a polyacrylamide gel (Biogel P 60, 50-150 mesh exclusion limit >60,000 Bio-Rad Laboratories, California) in 0.05 M tris buffer, pH 8.0, containing 0.08% (v/v) Tween 80 and 0.1% (v/v) 2-mercaptoethanol to stabilize the enzyme. Column 60 X 4 cm. Flow rate 20 ml/hr, 4 ml fractions. (A) OD at 280 nm, ( ) OD at 540 nm, ( ) LDH assay with p-nitrophenyl phosphate for AcP. From Hopkinson and Harris (85).

Icteric speciments are not suitable for use. Bilirubin at 6 mg/dl or 103 xmol/l causes an average bias of +2.2 U/1. Determing tartrate blank-corrected acid phosphatase activity (AcP minus AcP Blank) will greatly reduce or eliminate bilirubin interference. 

Panteghini M, Pagani F. Reference intervals for two bone-derived enzyme activities in serum bone isoenzyme of alkaline phosphatase (ALP) and tartrate-resistant acid phosphatase (TR-ACP). Clin Chem 1989 35 181-1. 

ACP = acyl carrier protein ACPA D = ACPA desat-urase AlkB = octane 1-monooxygenase AOX = alternative oxidase DMQ hydroxylase = 5-demethoxyquinone hydroxylase EXAFS = extended X-ray absorption fine structure spectroscopy FMN = flavin mononucleotide FprA = flavoprotein A (flavo-diiron enzyme homologue) Hr = hemerythrin MCD = magnetic circular dichroism MME hydroxylase = Mg-protophorphyrin IX monomethyl ester hydroxylase MMO = methane monooxygenase MMOH = hydroxylase component of MMO NADH = reduced nicotinamide adenine dinucleotide PAPs = purple acid phosphatases PCET = proton-coupled electron transfer, PTOX = plastid terminal oxidase R2 = ribonucleotide reductase R2 subunit Rbr = rubrerythrin RFQ = rapid freeze-quench RNR = ribonucleotide reductase ROO = rubredoxin oxygen oxidoreductase XylM = xylene monooxygenase. 

Pantothenic acid occurs in foods both in the free form and bonded to coenzyme (CoA) or acyl carrier protein (ACP) therefore hydrolysis is needed to extract it totally. Since it is degraded by acid and alkaline hydrolysis, only an enzymatic digestion can be applied. Enzyme hydrolysis with papain, diastase, clarase, takadiastase, intestinal phosphatase, pigeon liver pantetheinase, or combination of them has been used. 

Vitamin B5 occurs in three biologically active forms in foods [1] pantothenic acid, coenzyme A (CoA), and acyl carrier protein (ACP). Calcium or sodium pantothenate are the forms generally used as supplements in infant formula [4], The total quantification of vitamin B5 requires the release of pantothenic acid from CoA and ACR Since it consists of pantoic acid linked through an amide linkage to p-alanine, chemical hydrolysis cannot be used. The only alternative to free pantothenic acid from CoA is the digestion with a number of enzymes (pepsin, alkaline phosphatase, pantetheinase) nevertheless, this treatment is unable to release the vitamin from ACP [27,28]. For the extraction of free pantothenic acid from milk and calcium pantothenate from infant formula an acidic deproteination is often used, followed by centrifugation and filtration [29,30]. 

LIST OF ABBREVIATIONS ACP, acyl carrier protein 5ALA, 5-aminolevulinic acid AU, 6-azauracyl CAP, chloramphenicol CHI, cycloheximide DCIP, 2,6-dichlorophenolindo-phenol DCMU, 3-(3,4-dichlorophenyl)-1,1-dimethyl urea DG, digalactosyl-diglyceride DPC, diphenylcarbazide ETS, electron-transport system FDPase, alkaline fructose 1,6-diphosphate phosphatase G-3-P, glyceraldehyde-3-phosphate MG, monogalactosyldiglycer-ide PSI, PSII, photosystems I and II P700, active center of photosystem I PMS, phenazine methosulfate Q, photosystem II quencher Ru-l,5-diP, ribulose-1,5-diphosphate SDS, sodium dodecylsulfate SL, sulfolipid. 

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