Вы находитесь на странице: 1из 5

CLIN. CHEM.

30/3, 364-368 (1984)

Chemical and Clinical Evaluation of the Random Access Analyzer


“RA-1 000”
Morton K. Schwartz,1 Bernard E. Statiand,2 Joan Coughlin,3 Cariotta Eisen,’ Martin Fielsher,’ Ralph Ito,2
Jacob B. Levine,3 Ronald Ng,2 Gina M. Pennachia,1Herbert N. Rose,3and Kathy Woolsey2

In the RA-1000, a random-access discrete analyzer, an inert a relative (to water) density of 1.9, it settles to the bottom of
fluorocarbon fluid is used to prevent interaction and car- the cuvette. The analytical reaction that takes place in the
ryover. Production-model instruments were evaluated in two cuvette can be monitored by colorimetric or ultraviolet
laboratories with respect to determination of glucose, creati- detection, with the use of direct end-point or initial or
nine, total protein, inorganic phosphorus, cholesterol, alka- kinetic rate reactions. The probes are raised and moved
line phosphatase, lactate dehydrogenase, creatine kinase, y- horizontally while the reagent and sample trays rotate to a
glutamyltransferase, and aspartate and alanine aminotrans- position appropriate for the next analysis. Back-and-forth
ferases. Within-run, among-run, and day-to-day (for 15 days) and stop/start rotation of the reaction tray mixes the sam-
precision was assessed, and results were correlated with ples with the reagents.
With the RA-1000, random access analysis is possible at
those obtained by the methods routinely in use in our
an analytical rate of 240 assays per hour. The operator’s role
departments. Precision was excellent, correlation accept-
is merely to place samples in the cups, ensure that reagent
able. containers are in place, and then request analysis, identify-
ing the specimen through the computer keyboard. Calibra-
In 1982, Technicon Instruments Corporation introduced a
tion, test-result analysis, detection of machine problems,
new generation of automated chemical analyzers (1). This
and calculation of results are all done by the computer.
instrument, the “RA-lOOO,” permits rapid “random-access”
Our evaluation of this instrument, reported here, includ-
clinical analysis without the limitation of cross-contamina- ed studies of the precision of the methods, linearity of the
tion (carryover) that exists at both sampling and reagent
procedures, and correlation of the values generated by the
probe in all previously described continuous-flow and many
RA-1000 with those obtained in our respective clinical
discrete clinical analyzers. In the RA-1000, an immiscible,
laboratories by our routinely used methods.
nonreactive fluid is used as a positive barrier between
sample and reagent and the interior and exterior surfaces of Materials and Methods
the respective probes. This fluorocarbon material provides
an inert, deformable surface that prevents carryover and The production-model HA-bOO and reagents we used in
ensures accurate delivery. In operation, the adjacent aque- these studies were provided by the manufacturer. The tests
ous liquids have contact only with the fluorocarbon and not we evaluated included alkaline phosphatase (EC 3.1.3.1) (2),
with the solid surface of the tubing or other fittings on the alanine and aspartate aminotransferases (EC 2.5.1.2 and
instrument. 2.6.1.1) (3), cholesterol (4), creatine kinase (EC 2.7.3.2) (5),
The instrument consists of sample probes and reagent creatinine (6), glucose (7), lactate dehydrogenase (EC
probes, which operate through Hamilton-type syringes; a 1.1.1.27) (8), total protein (9), inorganic phosphorus (10), and
circular 30-position sample tray; a reagent tray (maximum y.glutamyltransferase (EC 2.3.2.2) (11). We selected these
of 14 reagent containers); a 100-position reaction tray; and a tests for assessment because they represent the several
computer, which controls the operation. types of assays that can be accommodated in the RA-1000:
those depending on direct and end-point reactions (total
In operation, the sample- and reagent-probes are initially protein, inorganic phosphorus, glucose, cholesterol), kinetic
positioned over their respective trays with the syringes in rate reactions (y-glutamyltransferase, alkaline phospha-
the discharged position but with the reagent lines ifiled with tase, creatine kinase, lactate dehydrogenase, and the amino-
the fluorocarbon. A small air bubble is aspirated into each transferases), and initial rate reaction (creatinine).
probe, and the probes are then lowered into the sample cup The instruments used in the comparative studies (at the
and reagent container. Sample and reagent are aspirated respective laboratories) were the szsc (Technicon Instru-
into the tubing by the syringe pumps. The computer controls ments Corp.)’; the Cobas-Bio centrifugal analyzer (Roche
aspiration of a specified volume of sample (2.5-30 pL) and Analytical Instruments, Nutley, NJ 07110)1; the Astra 8
reagent (325-375 pL) through the syringes and into the (Beckman Instruments, Inc., Fullerton, CA 92834)3.2; the
tubing. The probes are then raised, moved horizontally, and aca discrete analyzer (Du Pont Instruments, Wilmington,
positioned over the reaction cell cuvette, on the reaction DE 19898)2; the Multistat analyzer (Instrumentation Labo-
tray. The probes are lowered into this cuvette, and sample ratory, Lexington, MA 02173)2; and the AutoAnalyzer LI
and reagent are discharged by the syringe pumps. A small (Technicon)2.
amount of the fluorocarbon is also introduced into the In our evaluation, we determined precision according to
cuvette by a peristaltic pump. Because the fluorocarbon has NCCLS guidelines (12). For use in the precision studies, six
reference materials with analyte concentrations extending
through the analytical range of the assays were provided by
‘Department of Clinical Chemistry, Memorial Sloan-Kettering Techmcon [Beta SMAC calibrator, RA-1000 calibrator, TQC
Cancer Center, New York, NY 10021. Hi, TQC Lo (linearity controls), and Alert 1 and Alert 2
2Department of Laboratory Medicine, Boston University Hospi-
tal Medical Center, Boston, MA 02118. (assayed controls)]. One group2 also used control specimens
3Technicon Instruments Corp., Tarrytown, NY 10591. with two analyte concentrations, provided by the Quality
Received July 18, 1983; accepted November 14, 1983. Control Survey Program of the Massachusetts Pathology

364 CLINICAL CHEMISTRY, Vol.30,No. 3, 1984


Society. The other group’ also used unassayed
materials sion for replicate samples in each category. All coefficients of
from Ortho Diagnostics and Hyland Diagnostics,
the same variation were acceptable, and the mean values obtained
as they use in their general quality-control program. with the two instruments did not differ significantly. The
The precision studies involved two experiments on each of highest CVs in the within-run experiments were seen at low
15 days, in which all of the reference materials were assayed activities of enzymes. In several instances, a large variation
in duplicate. Thus at each clinical laboratory there were was observed for high values of creatine kinase activity, for
eight different controls x two aliquots per experiment x two “in-house” quality-control specimens prepared from lyophil-
experiments per day x 15 days, for a total of 480 observa- ized material early in the work day and allowed to stand in
tions per method. The aim was to have analytes at three the refrigerator until the afternoon precision experiment, a
concentrations that would span the linear range of the practice not ordinarily followed. In many instances, the CVs
method, and to evaluate both total precision and its day-to- in the total-precision studies were higher. However, for most
day, among-run, and within-run components. constituents, the CVs were <2.5%. We conclude that the
In the correlation studies, we were guided by a proposed precision of this instrument equals or exceeds the multi-
NCCLS standard (13). channel variability, medically significant required preci-
sion, or intralaboratory variability reported in surveys of
Results referee or university hospitals (Table 2).
Precision. Table 1 summarizes within-run and total preci- Correlation. Table 3 summarizes the correlations between

Table 1. PrecisIon for the RA-1000 with Control Materials


Within-run precIsIon: man analyt. value (and CV, %)
Analyte InstitutIon Alert 1
Beta Alert 2 TQC HI RA-1000 cal TQC Lo In-house a In-house 2
Glucose,mg/L 1b 2240 (0.8) 720 (0.9) 3050 (0.9) 4130 (0.9) 2390 (0.7) 460 (1.1) 2690 (0.6) 990 (0.7)
Creatinine, mg/L 1 49(0.9) 15 (2.8) 89 (0.8) 182 (2.4) 90(0.8) 9 (4.7) 51 (1.9) 10 (4.4)
2 49(0.9) 15 (2.0) 89 (1.0) 182 (2.1) 91(0.5) 9 (4.9) 16 (1.8) 52 (1.4)
Totalprotein, g/L 1 57(0.7) 68 (1.3) 55 (0.8) 86 (0.8) 60(0.7) 26 (1.6) 81 (0.7) 61(1.1)
2 57(0.7) 70 (1.0) 55 (0.8) 85 (0.7) 60(0.7) 26 (1.1) 71 (0.6) 51(1.2)
Phosphorus,mg/L 1 56 (1.1) 64 (0.7) 58 (0.8) 82 (1.2) 55 (0.8) 10 (3.2) 71 (0.6) 37 (1.2)
2 58 (0.5) 63 (1.1) 59 (0.8) 88(0.7) 58 (0.5) 13 (2.3) 41 (1.0) 78 (2.2)
Cholesterol, mg/L 1 1840 (2.6) 1900 (2.7) 1200 (3.2) 2400 (1.5) 1840 (0.9) 460 (2.3) 2560 (1.3) 1540 (2.6)
2 1890 (0.7) 1930 (2.3)1230 (1.7) 2450 (1.1) 1870 (0.7) 460 (1.9)2490 (1.0)1300 (3.5)
Alk. phosphatase, U/L 1 77 (0.8) 48 (3.3) 182 (1.5) 480(1.2) 104 (1.2) 13 (4.8) 235 (1.1) 83 (4.0)
2 83(0.7) 57 (2.7) 194(1.4) 510(1.1) 111 (0.9) 14 (4.1) 75 (2.1) 183(1.9)
Asp. aminotransferase, U/L 1 152 (1.7) 37 (2.7) 185 (1.5) 286 (1.5) 131 (1.6) 11(10.7) 78 (2.2) 13 (7.1)
2 164 (0.8) 36 (2.5) 199 (1.6) 307 (1.1) 140 (0.9) 13 (6.1) 36 (2.9) 100 (1.8)
Ala. aminotransferase, U/L 1 118 (2.0) 18 (4.8) 145 (1.8) 160(1.3) 76 (2.0) 8 (12.6) 81 (2.8) 18 (6.2)
2 128 (1.0) 18(16.4) 154(1.0) 160(1.5) 80(1.4) 11 (8.9) 31(10.5) 118(1.4)
Creatine kinase, U/L 1 598 (0.8) 148 (1.8) 516 (1.2) 713 (0.8) 508 (0.9) 88 (2.9) 291 (3.4) 155 (1.4)
2 632 (0.4) 148 (2.1) 522 (2.3) 737 (0.8) 506 (0.8) 91 (1.8) 125 (1.3) 428 (6.3)
Lactate dehydrogenase, U/L 1 275 (2.4) 120 (2.3) 397 (0.7) 370(1.4) 115 (1.6) 85 (2.2) 314 (1.6) 140 (1.2)
2 294 (0.4) 129 (2.2) 430 (0.8) 392 (1.2) 120 (1.1) 85 (1.3) 173 (1.2) 409 (1.2)
-Glutamyltransferase, U/L 1 164 (1.1) 29 (2.3) 115 (3.1) 219 (1.0) 135 (1.7) 31 (2.9) 134 (1.8) 25 (2.9)
2 176 (0.3) 27 (1.8) 124 (1.7) 237 (0.7) 145 (0.9) 33 (1.8) 59 (0.9) 137 (1.6)
aThe ‘in-house’ materialdifferedforthe two institutions.
blflStjtUtiofl 1 is M.S.K., institution 2 is B.u.M.c.

Table 1. Continued
Total precisIon: mean analyte value (and CV, %)
Beta Alert 1 Alert 2 TQC HI RA-1000 cal TOC Lo In-house 1 #{149} In-house 2
2240 (1.4) 720 (1.3) 3050 (1.3) 4130(1.7) 2390(1.1) 460 (1.6) 2690 (1.9) 990 (1.4)
49(1.1) 15(2.8) 89(1.0) 182 (2.5) 90(1.2) 9 (4.7) 51 (1.9) 10 (5.3)
49 (1.5) 15 (2.0) 89 (1.6) 182 (2.5) 91(1.3) 9 (4.9) 16 (1.8) 52 (1.8)
57(0.7) 68 (2.3) 55 (0.8) 86(0.8) 60(1.1) 26 (1.6) 81 (0.7) 61 (1.1)
57(0.5) 70(1.7) 55 (0.8) 85(0.7) 60(0.8) 26 (1.6) 71 (0.7) 51 (1.2)
56(1.1) 64(1.0) 58(1.2) 82(1.5) 55(0.9) 10 (4.3) 71 (1.9) 37 (1.4)
58 (0.5) 63(1.1) 59 (0.7) 68(1.0) 58(0.9) 13 (2.3) 41 (1.0) 78 (2.2)
1840 (2.6) 1900(2.7) 1200 (3.3) 2400(1.5) 1840 (1.4) 460 (2.5) 2560 (1.4) 1540 (2.6)
1890 (1.0) 1930 (2.4) 1230 (1.7) 2450(1.4) 1870 (1.1) 460 (2.3) 2490 (1.2) 1300 (3.7)
78 (1.4) 48 (8.2) 182 (2.7) 480 (1.3) 104 (1.9) 13 (5.3) 235 (1.6) 83 (6.4)
83(1.6) 57(7.1) 194 (1.6) 510 (1.2) 111 (1.6) 14 (5.7) 75 (3.5) 183 (2.1)
152 (1.9) 37(8.4) 185 (2.4) 86 (1.8) 131 (2.3) 11(12.6) 78 (2.6) 13 (10.1)
164 (0.9) 36 (6.6) 199 (1.6) 307 (1.3) 140 (1.3) 13 (6.2) 36 (3.3) 100 (2.2)
118 (2.1) 18 (8.8) 145 (2.2) 150 (1.6) 76(2.6) 8(13.9) 81 (2.8) 18 (8.3)
128(1.3) 18 (7.6) 154 (1.3) 160(1.5) 80(1.9) 11(10.0) 31 (10.8) 118 (1.8)
598 (1.1) 148 (6.0) 516 (5.5) 713 (1.8) 508 (2.5) 88 (3.3) 291 (7.7) 155 (6.6)
632 (1.7) 148 (5.3) 522 (5.1) 737 (2.1) 506 (2.6) 91 (4.1) 125 (4.8) 428 (8.5)
275 (2.5) 120 (2.5) 397 (1.5) 370 (1.6) 115 (2.1) 85 (2.2) 314 (1.7) 140 (1.9)
294 (1.0) 129 (2.2) 430 (1.2) 392 (1.3) 120 (1.4) 85 (4.1) 174 (1.6) 409 (1.7)
164 (1.9) 28 (8.4) 115 (3.1) 219 (2.2) 135 (2.2) 31 (3.4) 134 (2.2) 25 (3.0)
176 (1.2) 27 (8.4) 124 (1.9) 237 (1.5) 145 (1.5) 33 (2.1) 59 (1.7) 137 (2.0)

CLINICAL CHEMISTRY, Vol. 30, No. 3, 1984 365


Table 2. Comparison of Precision (CV5) Obtained with the RA-1000 for Beta Material and In-House
Control Materials I and 2
Constituent PA-bOO suac 1975-1979 CAP 33 unIversity MedIcally SIgnIficant
(14) Survey(15,16) hospitals (1?) signIficant (18) percentage
In house (Enzymes 1978-1981) thang.
Beta 1 2 between days
(f9)b

Glucose MSK 1.4 1.9 1.4 2.1 3.6 3.1 5.0 6


Creatinine MSK 1.1 1.9 5.3 4.5 7.6 7.8 5.3 15 (0.014)
BU 1.5 2.0 1.8 5.5 (0.031)
Total protein MSK 0.7 0.7 1.1 1.8 2.4 2.6 4.3 9.5 (18)
BU 0.5 0.7 1.2 7.5 (61)
Phosphorus MSK 1.1 1.9 1.4 3.6 4.7 4.9 5.6 6
BU 0.5 1.0 2.2
Cholesterol MSK 2.6 1.4 2.6 3.2 4.7 5.1 8.0 7
BU 1.0 1.2 3.7
Alk. phosphatase MSK 1.4 1.6 6.4 8.8 4.6 (100) 10.6 3.2 13 (79)
BU 1.6 3.5 2.1 3.8 (200) 11 (206)
Asp. aminotransferase MSK 1.9 2.6 10.1 2.1 10.2 (40) 11.8 8.0 24 (35)
BU 0.9 3.3 2.2 7.2 (80) 10 (112)
Ala. aminotransferase MSK 2.1 2.8 8.3 7.7 (40)
BU 1.3 10.8 1.8 5.3 (80)
Creatine kinase MSK 1.1 7.7 6.6 6.0 13.2 (180)
BU 1.7 4.8 8.5 11.0 (360)
Lactate dehydrogenase MSK 2.5 1.7 1.9 5.0 7.4 (200) 3.4 17 (146)
BU 1.0 1.6 1.7 5.6 (400) 14 (366)
y-Glutamyltransferase MSK 1.9 2.2 3.0
BU 1.2 1.7 2.0
#{149}
The numbers in parentheses in this column are the activities in U/L at whichthe meanCVs wereestimated.b Numbers in parentheses in this column are the
concentrationsor enzyme activity atwhich the changewas calculated (g/L or tilL).

Table 3. Correlation of RA-1000 Procedures with Techniques Routinely Used by MSKCC* and BUMC**
Mean values
Correlation
CorrelatIon No. of RoutIne Regression .quatlon coeffIcIent,
ConstItuent (ref.) method samples method RA-1000 (y = PA-bOO) r S,.1
Glucose (20) Astra 156 1170 1230 y = 1.06x - 7.1 0.998 37
Totalprotein(9) 132 63 63 y = 1.02x - 1.2 0.996 1.5
Totalprotein(21) *Cobas 71 65 64 y = 1.OOx - 1.9 0.996 1.7
Total protein (21) **iL Multistat 49 62 61 y = O.97x + 5.7 0.996 1.2
Creatinine (22) SMAC 134 21 20 y = O.94x - 0.1 0.998 1.3
Creatinine (6) *Astra 8 70 21 22 y = 1.04x + 0.1 0.998 1.4
Creatinine (6) #{176}#{176}Astra
8 50 48 48 y = I .03x - 0.7 0.996 5.6
Phosphorus (10) SMAC 131 37 38 y = 1.03x + 0.2 0.985 2.6
Phosphorus (10) Cobas 40 38 39 y = 0.93x + 3.8 0.981 3.6
Phosphorus (23) #{176}AutoAnal
Ii 44 40 42 y = 1.06x - 2.7 0.999 1.0
Cholesterol (4) SMAC 132 1790 1830 y = 1.02x - 1.2 0.996 1.7
Cholesterol(4) *Cobas 71 1850 1850 y = 1.OOx - 1.9 0.996 1.5
Cholesterol(24) **aca 49 2490 2460 y = O.97x + 1.7 0.996 1.2
Alk. phosphatase (25) #{176}swc 37 175 173 y = 0.96x + 4.9 0.992 9.8
Alk. phosphatase (26) **lL Multistat 59 119 172 y = 1.49x - 5.2 0.992 9.5
Asp. aminotransferase (27) *SMAC 70 41 38 y = 0.91x - 0.89 0.999 5.9
Asp. aminotransferase (28) *Cobas 125 47 44 y = O.99x - 2.50 1.000 3.4
Asp. aminotransferase (28) “IL Multistat 86 37 54 y = 1.62x - 8.44 0.999 7.8
Ala. aminotransferase (27) *5AC 116 35 42 y = 1.17x + 1.55 0.998 3.4
Ala. aminotransferase (28) *Cobas 65 32 36 y = 1.19x - 2.22 0.999 5.9
Ala. aminotransferaso (28) “IL Multistat 65 58 105 y = 1.88x - 3.60 0.999 6.3
Creatine kinase (29) *SMAC 128 73 90 y = 1.07x + 12.0 0.996 11.9
Creatine kinase (30) *Cobas 68 65 91 y = 1.18x + 14.2 0.998 8.3
Creatine kinase (30) **lL Multistat 60 158 330 y = 1.99x + 1.17 0.996 14.1
Lactate dehyd. (31) *SMAC 120 241 193 y = O.78x + 6.40 0.995 9.8
Lactate dehyd. (32) *Cobas 65 263 215 y = 0.79x + 7.07 0.998 9.9
Lactate dehyd. (32) **lL Multistat 60 195 320 y = 1.58x + 8.9 0.997 15.8
-Glutamyltrans. (32) *SMAC 118 102 92 y = 0.87x - 4.01 0.998 0.14
y-Glutamyltrans. (34) *Cobas 65 90 90 y = 0.85x + 0.16 0.998 0.13
-Glutamyltrans. (34) 58 149 100 y = 0.64x + 5.47 0.998 10.2
A11Multistatassayswere performed at 30 #{176}C.
Unitsfor glucose, creatinine,phosphorus,and cholesterol,mglL;totalprotein,g/L; all enzymes,tilL.

results obtained for the same specimen with the RA-1000 temperature results in a wide difference in slope, but the
and by the routine procedures mentioned above. We empha- correlation coefficients (r) were excellent.
size that all the routine comparison enzyme measurements As part of the evaluation, all of the correlation assays
at one institution2 were done at 30#{176}C,
whereas all RA-1000 were done in duplicate, by both the RA-1000 and the
assays were carried out at 37 #{176}C.
This difference in assay comparative methods. Table 4 lists the standard deviations

366 CLINICAL CHEMISTRY, Vol. 30, No. 3, 1984


where the demand is relatively small and large batch-type
Table 4. Precision of Duplicate Assays during instruments are not suitable. These advantages can only be
Correlation Studies acceptable if the precision and accuracy of the RA-1000 are
Standard deviation of duplicates at least equivalent to those available with established
Instrument Comparison systems.
compared RA-l000 Instrument From our evaluation of production-quality RA-l000s in
Creatinine our two laboratories, we conclude that total precision is as
SMAC 0.6 (133) 1.0 (130) good as that obtained with the comparison instruments. It is
Astra 0.4 (70) 0.4 (69) much better than is required as medically significant, and
Astra 0.7 (50) 0.6 (50) the intralaboratory precision is better than reported hither-
Total protein
SMAC 0.6(134) 0.6 (130) to. The degree of correlation with the methods used routine-
Astra 0.7 (72) 0.7 (68) ly in our respective laboratories indicates that the RA-1000
ILMultistat8 0.4 (49) 1.5 (49) will provide values for these analytes that compare favor-
Phosphorus ably with the routine values. Additional studies are now
SMAC 0.5 (131) 0.5 (127) underway, intended to establish the flexibility of the RA-
Cobas 0.5 (72) 0.8 (34) 1000 and its potential with respect to user-introduced meth-
AutoAnalyzer II 0.3 (42) 0.4 (44)
Cholesterol ods.
SMAC 19 (134) 30 (117) The RA-1000 is easy to operate. It was well received by
Cobas 20 (72) 30 (68) the technologists and re-calibration is required relatively
aca 13 (51) 26 (51) seldom. The instrument at one institution1 did not require
Alk. phosphatase calibration during six months of daily use; at the other,2 the
SMAC 0.7 (134) 4.8 (119)
instrument was calibrated arbitrarily once each week. Such
Cobas 1.7 (72) 4.3 (65)
ILMultistat 2.2 (60) 3.4 (57) stability of performance offers the laboratory a great savings
Asp. aminotransferase in calibration material. One RA-1000’ had no “down-time”
SMAC 1.1 (128) 2.8 (1 19) during the evaluation; it was in operation each day. The
Cobas 1.2 (70) 2.4 (68) other2 required one or two minor adjustments but gave very
ILMultistat 1.9 (86) 1.8 (86) satisfactory performance.
Ala. aminotransferase
SMAC 1.1 (126) 6.2 (81) We gratefully express our thanks to the Technicon Instrument
Cobas 1.1 (66) 0.9 (67) Corp. for support of this evaluation.
IL Muitistat 1.2 (64) 1.6 (65)
Creatine kinase
SMAC 2.2 (125) 4.4 (120) References
SMAC 1.7 (72) 1.3 (65)
IL Multistat 1.6 (55) 4.8 (63) 1. Smith J, Svenjak D, Turrell J, Vlastelica D. An innovative
Lactate dehydrogenase technology for “random-access” sampling. CIin Chem 28, 1867-1872
SMAC 2.2 (125) 4.4 (120) (1982).
Cobas 2.3 (70) 4.2 (65) 2. Tietz NW, Burtis C, Ervin E, et al. Progress in the development
IL Multistat 2.3 (58) 3.6 (60) of a recommended method for alkaline phosphatase activity mea-
y- Glutamyltransferase surements. Clin Chem 26, 1023 (1980). Abstract.
SMAC 2.0 (131) 3.7 (99) 3. Keiding R, Horder M, Gerhardt W, et al. (Committee on En-
Cobas 1.8 (69) 3.5 (62) zymes, Scand Soc for Clin Chem and Clin Physiol). Recommended
aca 1.6 (58) 4.5 (58) methods for the determination of four enzymes in blood. Scand J
A11Multistat
assayswereperformedat30 #{176}C. Clin Lab Invest 33, 291-306 (1974).
Units for creatinine, phosphorus, cholesterol, mg/L; total protein, g/L; all 4. Allain CC, Poon LS, Chan CSG, et al. Enzymatic determination
enzymes,ti/L. Numbersin parenthesesindicate the no. of samples for each of total serum cholesterol. Clin Chem 20, 470-475 (1974).
analyte and comparison. 5. Stromme JH, Theodorsen L, Horde M, et al. (Committee on
Enzymes, Scand Soc for Clin Chem and Clin Physiol). Recommend-
ed method for the determination of creatine kinase in blood. Scand
of the differences between duplicates measured in the RA- J Clin Lab Invest 36, 711-723 (1976).
1000 and in each of the correlation instruments. As can be 6. Jaff#{233}
MZ. Ueber den Niederschlag, welchen Pikrinsfiure in
seen, the precision of duplicates for all assays in the correla- normalen Ham erzeugt and ueber eine neue Reaction des Kreatin-
tion study, regardless of the instrument, was very good. ins. Z Physiol Chem 10, 391-400 (1886).
7. Leon LP, Chu DK, Stasiw RO, Snyder LR. New, more specific
Discussion methods for SMA 12/60 multichannel biochemical analyzer. In
Advances in Automated Analysi.s, Technicon mt Congress, 1976,
In the RA-1000 the use of an inert fluorocarbon has Mediad, Tarrytown, NY, 1977, pp 152-156.
eliminated most of the problems of carryover and cross 8. Richard AH, Lubinski RM, Vanderlinde RE. Studies on the
reaction that exist in continuous-flow instruments (35). The kinetic assay of lactate dehydrogenase activity. Clin Chem 21, 1018
instrument we evaluated can analyze by random access one (1975). Abstract.
or as many as 12 components at a rate of 240 assays per 9. Skeggs LT Jr, Hochstrasser H. Multiple automatic sequential
hour. Thus if one constituent is analyzed per sample the rate analyses. Clin Chem 10, 918-936 (1964).
is 240 specimens per hour, but if 10 constituents are 10. Amador E, Urban J. Simplified serum phosphorus analysis by
analyzed in each sample, the analysis rate is 24 per hour. continuous flow spectrophotometry. Clin Chem 18, 601-604 (1972).
Minimum sample volumes range from 2.5 L (for albumin) 11. Stromme JH, Theodorsen L, Gerhardt W, et al. (Committee on
Enzymes, Scand Soc for Clin Chem and Clin Physiol). Recommend-
to 25 L (for bilirubin or uric acid). Reagent volumes range
ed method for the determination of y.glutamyltransferase in blood.
between 350 and 375 L and the reactions can be run at ScandJ Clin Lab Invest 36, 119-125 (1976).
either 30 or 37 #{176}C.
The small sample and reagent require- 12. Kennedy JW, Carey RW, Coolen RB, et al. Proposed guidelines
ments plus the random access capability make the instru- for user evaluation of precision performance of clinical chemistry
ment particularly useful as a “back-up” for (e.g.) SMAC, devices (EP5-P). NCCLS Pub 2, 1-48 (1982). National Committee
particularly in the case of enzyme assays that require for Clin Lab Standards, Villanova, PA.
dilution, in emergency laboratories, and in laboratories 13. Westgard JO, Bauer S, Green M, et al. NCCLS Proposed

CLINICAL CHEMISTRY, Vol. 30, No. 3, 1984 367


Standard (PSEP-4), protocol for establishing performance claims for terol. Methods Enzymoi 3,392-394(1957).
clinical chemical methods. Comparison of methods experiment. 25. Morgenstern S, KesslerG, Auerbach J, et al. An automated p-
National Committee for Clin Lab Standards, Villanova, PA, 1979, mtrophenyl phosphate serum alkaline phosphatase procedure for
pp 1-15. the AutoAnalyzer. Clin Chem 11,876 (1965). Abstract.
14. Schwartz MK, Bethune VG, Fleisher M, et al. Chemical and 26. Bowers GN Jr, McComb RB. A continuous spectrophotometric
clinical evaluation of the continuous flow analyzer satc”. Clin method for measuring the activity of serum alkaline phosphatase.
Chem 20, 1062-1070 (1974). Clin Chem 12, 70-89 (1966).
15. Roes JW, Frazer MD. The state of the art and medical useful- 27. Kessler G, Rush EL, Leon L, et al. Automated 340 nm
ness based intenial quality control. Am J Clin Pathol 78, 578-586 measurement of SGOT, SGPT and LDH. In Advances in Automated
(1982). Analysis, Technicon mt Congress 1970, 1, Thurman Assoc, Miami,
16. Lohif MR, DiSilvio TV, Ross JW, et al. Analytic clinical FL, 1971, pp 67-74.
laboratory precision. State of the art of selected enzymes. AmJCiin 28. Henry RJ, Chiamori N, Golub OJ, Berkman S. Revised spectro-
Pathol 78, 634-643 (1982). photometric methods for the determination of glutamic-oxalacetic
17. Straumford JV Jr, Copeland BE. Clinical chemistry quality transaminase, glutamic-pyruvic transaminase and lactic dehydrog-
control values in thirty-three university medical school hospitals. enase. Am J Clin Pat/wi 34, 381-398 (1960).
Preliminary report. Ibid. 44, 252 (1965). 29. Siegal AL, Cohen PS. An automated determination of creatine
18. Barnett RN. Medical significance of laboratory results. Ibid. 50, phoephokinase. In Automation in Analytical Chemistry, Technicon
671-676 (1968). Symposia 1966, 1, NB Scova et al., Eds, Mediad Inc., White Plains,
19. Ross JW. Precision performance standards. Medical care and NY, 1967, pp 474-476.
peer review criteria. Pathologist 35, 193-198 (1982). 30. Rosalki SB. An improved procedure for serum creatine phos-
20. Kadish AH, Little RL, Steinberg PC. A new and rapid method phokinase determination. J Lab Ciin Med 69, 696-705 (1967).
for the determination of glucose by measurement of rate of oxygen 31. Morgenstern S, for R, Kessler G, Klein B. Automated deterini-
consumption. Clin Chem 14, 116-131 (1968). nation of NAD-coupled enzymes, determination of lactic dehydro-
21. Kingsley GR. The direct biuret method for the determination of genase. Anal Biochem 13, 149-161 (1965).
serum proteins as applied to photoelectric and visual colorimetry. J 32. Wacker WEC, Ulmer DD, Vallee BL Metalloenzymes and
Lab Clin Med 27, 840-845 (1942). myocardial infarction. N Engi J Med 255, 449-456 (1956).
22. Chasson AL, Grady HT, Stanley MA. Determination of creati- 33. Morgenstern S, Viastelica D, Kessler G. Automated kinetic
nine by means of automatic chemical analysis. Am J Clin Pat/wi 35, determination of gainma-glutamyl-transpeptidase. Clin Chem 22,
83(1961). 1224 (1976). Abstract.
23. Hurst RO. The determination of nucleotide phosphorus with a 34. Szasz G. A kinetic photometric method for serum y.glut.amyl
stannous chloride-hydrazine sulfate reagent. Can J Biochem 42, transpeptidase. Clin Chem 15, 124-136 (1969).
287- 292 (1964). 35. Steindel SJ, Schoudt P. An assessment of random access fluid
24. Stadtman TC. Preparation and assay of cholesterol and ergos- technology. J Clin Lab Automation 3, 319-326 (1983).

368 CLINICALCHEMISTRY,Vol.30, No. 3, 1984

Вам также может понравиться