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References

1. Fogh-AndersenN, Siggaard-Andersen 0, Lundsgaard FC, Wim- PD. Diode-array spectrophotometry for simultaneous mea- surementofhemoglobinpigments. Cliii Chim Acta 1987;166:283-9. berley

2. Siggaard-Andersen 0. Experiences with a new direct-reading oxygen saturation photometer using ultrasound for hemolyzing the blood. Scand J Clin Lab Invest 1977;37(suppl 146):45-50.

3. Siggaard-Andersen 0. The acid-base status ofthe blood. Copen-

7. Fogh-Andersen N, Siggaard-Andersen 0, Lundsgaard FC, Wim- barley PD. Spectrophotometric determination of hemoglobinpig- ments in neonatal blood. Clin Chim Acta 1987;166:291-6.

8. Adams ML, Schuster TM. Phosphate-dependenspectroscopic changes in liganded hemoglobin. Biochem Biophys Res Commun 1974;58:525-31.

9. Zijlstra WG, Buursma A, Zwart A. Molar absorptivities of

human hemoglobin 1983;54:1287-91.

in the visible spectralrange. J Appl Physiol

hagen: Munksgaard,

1974:80.

4. Siggaard-Andersen 0, N#{248}rgaard-PedeB,eRem J. Hemoglo- b i n p i g m e n t s , s p e c t r o p h o t o m e t r i c d e t e r m i n a t i o n o f o x y - , c a r b o x y and sulihemoglobin 1972;42:85-100. - , capillary blood. Clin Chim Acta in met-,

5. Zjjlstra WG, Mook GA. Medical reflection photometry. The Netherlands: Van Gorcum Ltd., 1962:47.

Assen,

6. Zijistra WG, Buursma A, Kook JN, Zwart A. Problems in the spectrophotometric determination ofHb02 andHbCO in fetal blood. In: Mass AHJ, Kofstad J, Siggaard-Andersen 0, Kokholm G, eds. Physiology and methodology of blood gases and pH. IFCC Work- shop.Copenhagen: Private Press, 1984:45-55.

1 0 . S i g g a a r d - A n d e r s e n 0 , W i m b e r l e y P D , G # { 2 4 8 } t h e n I , S i g g a a r Andersen M. A mathematical d - model of the hemoglobin-oxygen

dissociation

curve

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human

blood and of the oxygen partial

pressure as a function oftemperature. Clin Chem 1984;30:1646-51.

11. Dijkhuizen burg B, Zijlstra

P, Buursma A, Fongers TME, WG. The oxygen binding

Gerding

AM, Oese-

capacity

of human

haemoglobin. Hufner’s factor redetermined. 1977;369:223-.31.

Pflugers Arch

12. Zijlstra WG. Quantitative

evaluation of the oxygentransport

capability of human

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13. OSM 2 Hemoximeterusers’handbook.Copenhagen: Radiome-

ter, 1984:49.

CLIN. CHEM. 34/4, 754-757

(1988)

Amylase in Unne as Measured by a Single-StepChromolytic Method

Roger L Berthotf,’ EmIly S. Wlnn-Deen,2and David E. Brune’

We studied a new single-step direct chromolytic (Behring D.A.T.) for measuring urinary amylase

method (1,4-a-D-

Assay of amylase in urine

overlooked

in

the

laboratory

is a rapid

investigation

test that is often of hyperamylase-

glucan results

glucanohydrolase, EC with those by a similar,

3.2.1.1) activity, comparing

but

two-step,

procedure

that

mia (1,2). reportedly

In acute pancreatitis,

urinary

amylase

excretion

(3)

increases

above its

reference

interval

before

requires an auxiliary (coupling) enzyme. gave virtuallyidenticalrelative responses

The two methods to purified human

pancreatic

and

salivary

amylases.

Assay

of

four

quality-

control materials to evaluate the total of the new method yielded CVs of 4 to

(day-to-day) precision 7%, similar to those of

the comparison method for each of the samples. Amylase activity was measured

four quality-control by both methods in

110 sion

random analysis

(i.e., untimed) urine specimens. provided a slope and y-intercept

Linear regres- of 0.947 and 4

U/L (x = ly, and

comparison a standard

method, y = direct method), error of the estimate of

respective- 25 U/L for

specimensin which the

amylase activitiesrangedfrom 11

to

1465

U/L

(mean

=

358

U/L)

by

the

comparison

method.

The

serum finding

amylase does and of a non-elevated

remains urinary

increased

longer. Also,

the

amylase

excretion rate

can

provide a rapid presumptive diagnosis of macroainylasemia

as the

source of

increased

serum

amylase

in

some

patients

(4, 5). The clinical

use of, and problems associated

measurement

of aniylase

been reviewed

elsewhere

activity

(6).

A

in serum and urine

common

deficiency

of

with, have amy-

lase assays is the lack of

urinary

excretion

rate

a normal reference interval

of

amylase

as

measured

for

the

by

the

method. Most of the methods devised for measuring

amylase

activity in of amylase McCroskey

serum or urine

involve, as a first step, the action

on

a poly-

et

al. (10)

or oligosaccharide

described

a

method

(7-9). For example,

in

which

amylase

mean rate of amylase excretion in 2-h timed from 95 healthy volunteers, as measured by

urine specimens the new method,

cleaves p-nitrophenyl

derivatives

of penta- and

to

yield

smaller

derivatized

oligosaccharides;

hexaosides then, in a

was 7.18 (SD

=

3.18) U/h, and the nonparametric (95%

second reaction, glucosidase

(EC 3.2.1.20) liberates p-nitro-

confidence interval) reference interval was 1.6 to 15.2 Urn. We consider the new method a promising alternative to other kinetic assays that require the use of auxiliary enzymes.

phenoxide, which

is then

measured

spectrophotometrically.

Recently, a obviates the

primary need for

substrate has been synthesized that

the

glucosidase-catalyzed

reaction:

Addltlenal Keyphrases: referenceinterval compared

two-stepprocedure

maltotriose,

covalently

bound

(CNP). The reaction

scheme with

to this

2-chloro-4-nitrophenol substrate is as follows:

5 CNP-a-G3

3CNP+

2CNP-a-G2+

3G3+

2G

1 Department of Pathology, Box 168, University of Virginia

Medical Center, Charlottesville,VA 22908. 2Present address:SD! Diagnostics, 11199Sorrento Valley Road,

San Diego,CA 92121. Received November 16, 1987;acceptedJanuary 4, 1988.

where G2 is maltoside,G3is maltotrioside,

and G is glucose.

The liberated

CNP

is measured

by its absorbance

at 405 run.

Because there is no requirement

for a second reaction

scheme, the or D.A.T.

method

has been

termed

“Direct

Amylase

in this Test,”

754 CLINICALCHEMISTRY, Vol. 34, No. 4, 1988

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