Amino Acid Analyzers - 071024093325
Amino Acid Analyzers - 071024093325
EXECUTIVE SUMMARY
Comparison Chart
Amino Acid Analyzers
This Product Comparison covers dedicated amino acid analyzers that can be used in the clinical laboratory. The chart lists specifications for the major components of each model;
however, for most models, various configurations are available. Amino acid analysis uses high-performance liquid chromatography (HPLC) techniques; many models listed in the
chart can also be used for other HPLC applications.
Amino acid analyzers detect and quantify primary and secondary amino acids in physiologic fluids such as plasma and urine to confirm diagnoses and monitor treatment of inborn
metabolism errors and of other disorders. These disorders are usually genetically produced errors in protein metabolism and can have serious complications if not detected and
treated early. The most common disorder is phenylketonuria (PKU), in which an enzyme deficiency results in increased concentrations of phenylalanine. PKU occurs an average of
once in every 10,000 births and is associated with mental retardation, seizures, and eczema. Other aminoacidurias include tyrosinemia, alkaptonuria, homocystinuria, and
branched-chain ketoaciduria (maple syrup urine disease), in which an enzyme defect in the decarboxylation of branched-chain α-keto acids increases concentrations of leucine,
isoleucine, valine, and alloisoleucine. Changes in amino acid levels can also be caused by starvation, injury, sepsis, liver or renal failure, and cancer.
Amino acid analyzers can also detect neurochemically active amino acids (aspartate, glutamate, and α-aminobutyric acid) in cerebrospinal fluid and can be used to assess the
nutritional status of patients before surgery as well as to follow the progress of their treatment.
The following device term and product code listed in ECRI’s Universal Medical Device Nomenclature System™ (UMDNS™) is covered:
Comparison Chart
Amino Acid Analyzers
Purpose
Amino acid analyzers detect and quantify primary and secondary amino acids in physiologic fluids such as plasma and urine to confirm diagnoses and monitor treatment of inborn
metabolism errors and of other disorders. These disorders are usually genetically produced errors in protein metabolism and can have serious complications if not detected and
treated early. The most common disorder is phenylketonuria (PKU), in which an enzyme deficiency results in increased concentrations of phenylalanine. PKU occurs an average of
once in every 10,000 births and is associated with mental retardation, seizures, and eczema. Other aminoacidurias include tyrosinemia, alkaptonuria, homocystinuria, and branched-
chain ketoaciduria (maple syrup urine disease), in which an enzyme defect in the decarboxylation of branched-chain α-keto acids increases concentrations of leucine, isoleucine,
valine, and alloisoleucine. Changes in amino acid levels can also be caused by starvation, injury, sepsis, liver or renal failure, and cancer.
Amino acid analyzers can also detect neurochemically active amino acids (aspartate, glutamate, and α-aminobutyric acid) in cerebrospinal fluid and can be used to assess the
nutritional status of patients before surgery as well as to follow the progress of their treatment.
Principles of Operation
Amino acids are organic compounds containing an amino group (NH2) and a carboxyl group (COOH), which are linked by peptide bonds to form proteins. Many are synthesized by the
body, while others are supplied in the diet. The important feature in separating amino acids is their basic structure: they are highly polar substances and exist in aqueous solutions as
dipolar ions called zwitterions, which have both negatively and positively charged groups. The amino acids' functional group (R), as shown in Figure 1, is used to distinguish one amino
acid from another. Primary, or α, amino acids have the amine group attached to the α, or first, carbon atom adjacent to the carboxyl group; secondary, or ß, amino acids have the
amine group attached to the ß, or second, carbon atom (see Figure 2). Some analyzers separate only primary amino acids, while others separate both primary and secondary amino
acids.
Before chromatographic analysis, the peptide bonds are dissolved in a solvent, and the sample is typically reacted
with phenyl isothiocyanate in a buffer to form a phenylthiocarbamyl (PTC) derivative. The PTC amino acids are
converted to phenylthiohydantoin amino acid derivatives that are then separated by chromatography and react with a
reagent, such as ninhydrin, forming a colored compound.
Chromatography separates sample components based on differences in their relative affinities for different media,
which are divided into two phases: stationary and mobile. Automated amino acid analysis requires HPLC, which uses
a liquid mobile phase forced through a column by a high-pressure pump. Sample injection can be automatic or
manual. The column contains the stationary phase, which in HPLC is composed of a liquid bound to a solid or a liquid
through which the mobile phase percolates.
There are five basic HPLC techniques: adsorption, partition or bonded phase, reversed phase, ion exchange, and size
exclusion. Adsorption chromatography separates components by differences in solubility and binding strength to the
adsorbent. In partition-phase chromatography, the stationary and mobile phases are immiscible liquids, and the
components are separated according to their solubility ratios in the two phases. Reversed-phase chromatography is
similar to the partition technique, except that the polarities of the two liquids are reversed. Ion-exchange
chromatography uses ion-exchange resins for the stationary phase and a buffer solution as the mobile phase. Size-exclusion chromatography uses a porous packing material that
retains larger molecules while allowing smaller ones to pass through, thereby separating components by molecular size.
The basic components of an HPLC system are a solvent reservoir, high-pressure pump, sample injector, analytical
column, detector, data recorder, and microprocessor. The solvent reservoir contains the mobile phase. The pump,
either single- or dual-piston reciprocating, contains a cam or gears that drive a piston into and out of the pump. In the
fill mode, the piston is withdrawn from the chamber, and liquid is drawn from the solvent reservoir into the pumping
chamber. In the pumping mode, the inlet check valve closes, and the outlet valve opens as the piston drives the
liquid into the column. A disadvantage of this type of pump is the pulsing nature of the solvent flow; however, most
systems incorporate a damping mechanism that controls this effect. The pumps in amino acid analyzers most
frequently use pressures from 1,000 to 3,000 pounds per square inch (psi).
The sample injector introduces the sample into the column. The fixed-loop injector, the most widely used type, is filled
using a noncalibrated syringe; the sample volume is dictated by the size and internal diameter of the sample loop.
Variable-volume injectors use a calibrated syringe to inject a precise volume into the loop.
The analytical column contains the stationary phase and is the most important part of the separation system. Usually composed of stainless steel that can withstand pressures up to
10,000 psi, the column ranges from 10 to 150 cm in length and from 2 to 5 mm in internal diameter. Column packing material should have minimum dead volume (i.e., be tightly
packed) and ensure maximum efficiency (i.e., narrow peaks on the chromatogram). Two types of columns—the precolumn and the guard column—protect the analytical column. The
precolumn is located between the pump and the injection valve; in amino acid analysis, it separates derivatized amino acids. The guard column, located between the injector and the
analytical column, prolongs the life of the analytical column by collecting any particulate matter or debris that would otherwise accumulate there. HPLC columns are highly efficient
when used with small (3, 5, or 10 μm), porous particles. Particle size must be as uniform as possible for efficient columns and optimal operating pressures. Spherical and irregularly
shaped particles are available; columns packed with these seem to be more durable and can operate at lower pressures.
In ion-exchange LC, the stationary phase is an ion-exchange resin that separates compounds by the sign and magnitude of their ionic charges. An aqueous solution is used as the
mobile phase. The resins are highly polymerized supports consisting of hydrocarbons with ionized functional groups. Available in the form of beads or granular particles, they have an
exchangeable counterion, which carries a charge opposite from that of the functional group (i.e., cation exchangers contain acidic groups, and anion exchangers contain basic groups).
The sample cation (X+) of the cation exchange resin (often used for amino acids) competes with the mobile-phase ions (Y+) for ionic sites on the support. Figure 3 shows how the
counterions are replaced by sample cations and bind to the functional groups. The neutral molecules and anions flow through the column and separate from the attached sample
cations. Another ion of higher affinity or large amounts of the same counterion can be used to elute the sample cations, releasing the weakly bound cations first. This method also
incorporates a postcolumn reaction of ninhydrin with free amino acids, so the results can be detected in the visible range. Elution can also be adjusted by controlling the pH of the
mobile phase, depending on the stationary phase and sample ion that are being used in the column.
In reversed-phase LC, a derivatizing reagent is usually added to the sample before it enters the column. The mobile phase is polar and the stationary phase is nonpolar, thereby
allowing the amino acids to separate by their polar functional groups (amines), which in normal phase would adsorb too strongly to the silica. The nonpolar packings are hydrocarbons
chemically bound to a silica base, allowing the more polar compounds to separate first. One type of packing is octadecyl (C18 hydrocarbon bonded to silica particles), referred to as
ODS (octadecyl silica). The polar mobile phase can consist of acetonitrile, aliphatic alcohols, water, tetrahydrofuran, or mixtures of these solvents.
The detector quantifies compounds as they elute from the column by relying on changes in the bulk property of the mobile phase and the sample constituents, such as the refractive
index (color change), or on some characteristic property of the sample constituent, such as fluorescence or ultraviolet absorption. The most widely used detector is the fixed- or
variable-wavelength ultraviolet-visible photometer, which can detect nanogram quantities. Another detector, the fluorometer, has a high sensitivity for fluorescent compounds and can
determine picogram quantities.
Amino acid analyzers are typically interfaced with a personal computer and proprietary software, which displays analysis data and the operating parameters of the unit in real time.
Depending on the unit, analysis data can either be printed for record-keeping or examination via a simple desktop laser printer, or, alternatively, the data can be stored on the
computer's hard drive. Many models allow for complex data management tasks, such as report making or statistical analysis.
Reported Problems
Problems can occur when buffers are contaminated with microorganisms, mainly Pseudomonas species, that exhibit dihydrolase activity for arginine and decarboxylase activity for
ornithine and lysine. This contamination can lead to a loss of arginine and can also affect other amino acid recoveries.
The storage of specimens for even 24 hours can alter the plasma amino acid levels; therefore, specimens should be analyzed as soon as possible. Because some derivatizing
reagents are unstable, derivatized amino acids must be assayed rapidly, and repeat testing may not yield reproducible results. Inaccurate results can also be caused by contamination
from a previous sample when using fixed-loop valves. The valve must be flushed with 5 to 10 loop volumes before loading.
The various standardization procedures have some limitations. External standardization is subject to variable sample losses—both during the preparative steps and before
chromatography analysis—as well as sample injection variability. Under normal conditions, the internal standard should not be present in the sample: the difficulty involved in
accurately measuring two peaks could limit precision.
The use of uncoated glassware in automated analyzers may pose a safety hazard to laboratory personnel because of the risk of breakage from solvent or buffer bottles. One
reported case involved a borosilicate glass bottle in an amino acid analyzer that exploded. The agency that reported the incident, the Scottish Home and Health Department, a branch
of the U.K. Department of Health, also recommends that laboratories considering the use of plastic-coated glassware check with the supplier to determine whether the glassware is
suitable for its intended applications, since different plastic coatings resist chemicals differently, have assorted properties at varied temperatures and pressures, and have distinct
aging properties.
Purchase Considerations
ECRI Recommendations
The accompanying comparison chart includes ECRI's recommendations for minimum performance requirements for amino acid analyzers.
Facilities purchasing amino acid analyzers should take into consideration the automated features of the instrument. Certain automatic features are desirable to facilitate sample
analysis. For example, automatic sample injection is preferred to manual injection. Automatic sample injection eliminates the possibility of operator error and ensures that all samples
are treated in the same manner. Automated flushing after sample analysis ensures that the analyzer is properly prepared for each subsequent sample and that no crossover
contamination will interfere with readings. It is recommended that clinical laboratory analyzers be able to interface with a laboratory information system (LIS) in order to more easily
collect and report diagnostic test results. The analyzer should also be capable of displaying results and other information both on a monitor and as a printout.
The sample column should be made with a rustproof material to ensure longevity of the column. The column should generally have a length of 10 to 150 cm and an internal diameter
of 2 to 5 mm. The particle size should be as uniform as possible to ensure adequate separation of the sample. Dual-piston, single-piston, and syringe eluent pumps are all generally
acceptable. The pump should have a pressure limit of at least 2,000 psi. Because of the risk of infection involved with the handling of any body-fluid specimen, purchasers should
consider devices that minimize operator contact with specimens.
Other Considerations
Ideally, before making a purchase, facilities should evaluate the amino acid analyzers they are considering in their own clinical environment for a few weeks. On-site evaluation
enables laboratories to verify the characteristics of the instrument reported by the manufacturer (e.g., pump flow accuracy, detector sensitivity and stability) with the workload and
sample types that the laboratory normally handles.
Final regulations of the Clinical Laboratory Improvement Amendments of 1988 (CLIA) were published by the U.S. Department of Health and Human Services in February 1992. Under
the CLIA regulations, all clinical laboratories are required to obtain federally issued certificates. To acquire a certificate, a lab must meet all relevant standards, which are determined
by the complexity of the tests being performed. The standards set forth by CLIA apply to areas such as patient test management, quality control (QC), proficiency testing, personnel
qualifications, and quality assurance (QA) programs. Certification fees vary according to complexity level and test volume. There are different levels of complexity outlined in the CLIA
regulations with corresponding calibration and quality control requirements. These requirements have changed as of January 2003. More information can be found at the following
website: http://www.cms.gov/clia.
Before purchasing new equipment or upgrading existing equipment, laboratories should thoroughly investigate the CLIA regulations that apply to their facility and to the devices being
considered. In certain situations, purchasing or upgrading a device may change the complexity category of the procedures. This could require additional staff training and certification,
as well as changes in QC, proficiency testing, QA programs, and other laboratory procedures.
An important consideration is the system's computer interface capabilities. The effectiveness of the interface with the existing LIS or the hospital's central computer system is crucial
for inputting test data, verifying testing accuracy, and maintaining QC, calibration, proficiency testing, and patient files according to CLIA guidelines. Although CLIA does not mandate
computerized reporting systems in hospital laboratories, it does require laboratories to have a system in place to ensure compliance with CLIA performance standards for QC and QA
of patient testing instruments and procedures. An effective LIS interface is a fast and efficient way to manage the large volume of test data that a laboratory generates each day as
well as a convenient method of organizing and storing data needed to comply with CLIA and other inspection agencies' requirements.
Cost Containment
Because amino acid analyzers entail ongoing maintenance and operational costs, the initial acquisition cost does not accurately reflect the total cost of ownership. Therefore, a
purchase decision should be based on issues such as life-cycle cost, local service support, discount rates and non-price-related benefits offered by the supplier, and standardization
with existing equipment in the department or hospital (i.e., purchasing all analyzers from one supplier).
Facilities should negotiate the best price for consumables (e.g., reagents, calibration gases, controls), training programs, and service contracts at the time of purchase. They should
also retain the option to accept or reject the service contract at the end of the warranty period.
For further information on cost containment, customized analyses, and purchase decision support, readers should contact ECRI's Capital Guide Group.
Stage of Development
Reversed-phase LC has become widely accepted because it can reduce turnaround time without loss of sensitivity. In addition, some of the newer HPLC derivatizing reagents can
develop stable derivatives with amino acids. Online derivatization systems enhance sensitivity and reduce manual input. At least one manufacturer has developed a mass
spectrometry system for amino acid analysis. Mass spectrometry-based analysis permits higher throughput by reducing the time it takes for sample separations to take place.
Advanced microprocessors have allowed the development of completely automated amino acid analysis systems and have helped reduce turnaround time. Computer workstations
allow automatic generation of calibration curves from standards, automation of the chromatography system, rapid data input and test result storage, and data communication with
other computer systems in the laboratory and hospital. Analyzer technology has become sufficiently versatile to adapt to batch analysis and is therefore useful in diagnostic
applications and for research.
BIBLIOGRAPHY
Aoyama C, Santa T, Tsunoda M, et al. A fully automated amino acid analyzer using NBD-F as a fluorescent derivatization reagent. Biomed Chromatogr 2004 Nov;18(9):630-6.
Burtis CA, Ashwood ER, Bruns DE, eds. Tietz fundamentals of clinical chemistry. 6th ed. Philadelphia (PA): WB Saunders; 2007.
Domon B, Aebersold R. Mass spectrometry and protein analysis. Science 2006 Apr;312(5,771):212-7.
Kaspar H, Dettmer K, Chan Q, et al. Urinary amino acid analysis: a comparison of iTRAQ-LC-MS/MS, GC-MS, and amino acid analyzer. J Chromatogr B Analyt Technol Biomed Life
Sci 2009 Jul 1;877(20-21):1,838-46.
Pincus MR, McPherson RA. Henry's Clinical diagnosis and management by laboratory methods. 22nd ed. Philadelphia (PA): WB Saunders; 2011.
Poinsot V, Gavard P, Feurer B, et al. Recent advances in amino acid analysis by capillary electrophoresis. Electrophoresis 2012 Jan;33(1):14-35.
Rutherford SM, Gilani GS. Amino acid analysis. In: Curr Protoc Protein Sci 2009 Nov 58:11.9.1–11.9.37.
RESOURCE LIST
Comparison Chart
Amino Acid Analyzers
RELATED RESOURCES
UMDNS
Analyzers, Laboratory, Body Fluid, Amino Acid [15-090]
Manufacturer Biochrom Ltd Div Harvard Hitachi High-Technologies membraPure GmbH SCION Instruments
Bioscience America Inc ARACUS Artemis 6000
Biochrom 30+ LA8080
WHERE MARKETED Worldwide Worldwide Worldwide Worldwide
FDA CLEARANCE Yes No No No
CE MARK Yes Yes Yes Yes
PERFORMANCE
Type of reaction Postcolumn ninhydrin Postcolumn ninhydrin Postcolumn ninhydrin Postcolumn ninhydrin
Amino acids detected Primary, secondary Amino sugars with special Primary, secondary Primary, secondary
column
No. of components 2 >50 amino acids 20, 42, or 55 50
Analysis time, min 10-120 20-150 >60 Method dependent
SAMPLE INJECTOR
Model Biochrom Alias Built-in Alias A6200 autosampler
Injection modes Variable Variable; direct injection Manual, autosampler Variable
Sample type Physiological fluids (plasma, Protein hydrolysates, physiologic Free amino acids, protein Physiological fluids (plasma,
serum, urine, CSF), fermentation fluids, foodstuffs, cell culture hydrolysates, feedstuff, culture blood, urine, cell extracts), protein
media, infusion solutions, media media hydrolysates, food and feedstuff
oxidized and non-oxidized protein hydrolysates
hydrolysates, peptide
hydrolysates, drug hydrolysates,
food and feedstuff hydrolysates,
cosmetics, fertilizers
Sample volume, µL 1-5,000 0.1-100 1-35, 5-50, 100 0.1-999.9
Sample capacity 84 vials 200 vials 96 vials 120 vials
Vial size 100 µL, 200 µL, 1.5 mL 1.5 mL 1.5 mL 1.5 mL
Autoflushing User defined Yes Yes Yes
DERIVATIZING REAGENT Ninhydrin Ninhydrin Ninhydrin Ninhydrin
Online/manual Online Online, 2-part ninhydrin system Online Online
COLUMN
Model or variations Biochrom High-speed; standard; high- Li High Speed 75 x 4 mm, 4 µm CE Na or Li or K
resolution (MSUD, PKU); Li High Resolution
125 x 4 mm, 7 µm (physiological,
hydrolysate); Li Advanced plus
150 x 4.6 mm, 5 µm)
(physiological, hydrolysate); Na
High Speed 75 x 4 mm, 4 µm; Na
High Resolution 125 x 4 mm, 7
µm; Na Advanced 150 x 4.6 mm,
7 µm (feedstuff); K 125 x 3 mm, 4
µm (biogenetic amines)
Construction Polyetheretherketone (all PEEK) Stainless steel Stainless steel Stainless steel
Available lengths, cm 200 analytical column,100 Multiple available 75 (Li, Na), 125 (Li, Na, K), 150 3, 15, 17.5, 21
prewash column (Li, Na)
Internal diameter, mm 4.6 Not specified 3 (K), 4 (Li, Na), 4.6 (Li, Na) 4.6
Particle size, µm 8-9 analytical 3 4 (Li, Na, K), 5 (Li), 7 (Li, Na) 7
Sorbent type Strong cation exchange Ion exchange Ion exchange resin Ion exchange
polystyrene/divinylbenzene cross-
linked resin
ELUENT PUMP
Model Biochrom Built-in S100 A6100 pump
Pump type Dual piston, ceramic pump head Dual piston Dual piston Dual plunger
No. of pumps 2 2 1 or 2 2
Flow range, mL/min 0.08-2.16 0.001-9.999 0.01-10 0.0001-10
Data storage Hard drive, network dependent Not specified Hard drive Hard drive, LIMS
DETECTOR
Model Biochrom Built-in Not specified A6300
Type Visible Visible UV/Vis Integrated reactor and detector,
dual channel detector
Filter/grating Filter with beam splitter Grating No No
Available wavelengths, nm 440-570 440, 570 fixed 440, 570 440, 570
Light source Tungsten Tungsten LED LED
Drift, AU/hr <1 x 10^-3 <1 x 10^-3 Not specified <3 x 10-4
Noise, AUFS <1 x 10^-3 <1 x 10^-3 Not specified <200 µAU
Cell volume, µL 8 3.2 10 <80
Cell pathlength, mm 15 Not specified Not specified 20
Autozero Yes Yes Optional Yes
Others available Fluorescence (requires additional NA Not specified No
fluorescence detector)
POWER REQUIREMENTS 115/220 V, 50/60 Hz 115 V, 50/60 Hz 110-230 V, 50/60 Hz 100-250 V, 47-63 Hz
DIMENSIONS, H x W x L, cm Not specified Not specified 108 x 37 x 69 (42.5 x 14.6 x 27.2) 75 x 45 x 75 (29.5 x 17.7 x 29.5)
(in)
WEIGHT, kg (lb) Not specified Not specified 60 (133.3) Not specified
PURCHASE INFORMATION
List price $76,400-87,500 $85,000-95,000 $99,063 (€90,000) Not specified
Warranty 1 year Not specified 1 year 1 year
Year first sold 2010 2018 2013 2020
Fiscal year Not specified April to March January to December Not specified
OTHER SPECIFICATIONS Optional accelerated, high- Built-in automatic wash function; <0.3% RSD reproducibility of Configured to standard test
performance, or high-resolution 3 pmol detection using ninhydrin; retention time; ~1% RSD method; automated method; high
LC system screening methods; postcolumn reaction column reproducibility of peak area. pre-productibility; stability;
90 min to arginine with minimizes peak diffusion; 2-part resolution and separation
accelerated method, 125 min with ninhydrin delivery system efficiency; country of origin: EU.
high performance, 150 min with eliminates reagent degradation;
high resolution; uses 5 lithium built-in vacuum degasser; built-in
citrate buffers; qualitative and leak sensors; automated start-up
quantitative analysis of ≤56 and shut-down; battery backup;
amino acids and derivatives. front-panel access for routine
maintenance; Windows 2000/XP
operating system; optional linear
or step gradients.
UMDNS CODE(S) 15090 15090 15090 15090
LAST UPDATED April 2020<1> February 2020 January 2020 May 2023
Supplier Footnotes
Model Footnotes
Data Footnotes <1>Specifications updated using
manufacturer's website.
Manufacturer Sykam GmbH Sykam GmbH Waters Corp Waters Corp
S 433 S 633 ACQUITY ACQUITY H-Class
Construction PEEK, PTFE and PVDF PEEK, PTFE, Teflon AF Stainless steel Stainless steel bio-inert
Available lengths, cm Not specified Not specified 10 10
ELUENT PUMP
Model S 2100 S 633-P ACQUITY UPLC BSM ACQUITY UPLC QSM
Pump type Quaternary gradient pump Low pressure gradient pump and 4 independently driven, software- 2 independently driven, software-
reagent pump controlled pistons controlled pistons
No. of pumps 2 2 Single binary Single quaternary
Flow range, mL/min 0.01-10 0.0001-10 gradient pump, 0.01-2 0.01-2
0.0001-2 reagent pump
Degasser 4 channel 7 channel Not specified Not specified
Increment of flow setting, Not specified Not specified 0.001 0.001
mL/min
Flow precision, % <1 <0.1 0.15 0.075
Flow accuracy, % <0.1 <1 1 1
Pressure limit, psi ≤5,076 5,076 15,000 15,000
Gradient (multistep or Multistep Not specified Continuous Continuous
continuous)
No. of eluents ≤3 3 gradient buffers, 1 reagent 4 4
solution, 1 washing solution, 1
ninhydrine reagent, 1
autosampler washing solution
CONTROL SOFTWARE
Temperature controls Yes Yes Not specified Not specified
SAFETY FEATURES Control pump pressures, Not specified Not specified Not specified
temperatures and leakages
DATA MANAGEMENT
Software platform DataApex Clarity chromatography Not specified Empower 2 and 3 Empower 2 and 3
data station (CDS)
No. of components 32
Analysis time, min Not specified
SAMPLE INJECTOR
Model ACQUITY UPLC FTN
Injection modes Variable
Sample type Protein hydrolysates, culture
media, fermentation broth
ELUENT PUMP
Model Not specified
Pump type Not specified
CONTROL SOFTWARE
Temperature controls Not specified
DATA MANAGEMENT
Software platform Empower 3, Masslynx, Waters
Connect
Filter/grating Grating
Available wavelengths, nm 190-700
Light source Deuterium arc
Drift, AU/hr <5 x 10^-4
Noise, AUFS 6 x 10^-6 AU
Cell volume, µL 0.5
Cell pathlength, mm 10
Autozero Yes
Others available Photodiode and
fluorescence/Qda (Single
Quadrupole MS)
POWER REQUIREMENTS 110 V
DIMENSIONS, H x W x L, cm Not specified
(in)
WEIGHT, kg (lb) Not specified
PURCHASE INFORMATION
List price Not specified
Warranty Not specified
Year first sold Not specified
Fiscal year January to December
OTHER SPECIFICATIONS Includes comprehensive
chemistry package, method
documentation, and installation;
specifically tested for AAA
analysis; validation, compliance,
and quality assurance programs
available.