Scandinavian Committee Research Articles

“Calculate the Limits of the Possible”: Scandinavian Legal Diplomacy, Diplomatic Arenas and the Establishment of the Permanent Court of International Justice

Abstract This article considers the role of the Scandinavian states in the establishment of the Permanent Court of International Justice (pcij) and how the construction of the pcij and the wider League of Nations shaped Scandinavian legal diplomacy. It does so by analyzing legal-diplomatic practices within five significant diplomatic arenas between 1917 and 1920, from the early Scandinavian committee work, via the Advisory Committee of Jurists to the First League Assembly. Our article argues that we need to be attuned to how the emergence of the League of Nations and the particular sequence of multilateral negotiations that led to the creation of the pcij transformed Scandinavian (legal) internationalism and aligned the three countries to the new international order.

Calibration of the Ektachem Amylase method using human reference materials and the Phadebas Blue Starch method as an interim reference method.

In a multilaboratory study a consensus was established to calibrate the Ektachem Amylase method to reproduce the results of the Phadebas Blue Starch method. The calibration graph has a slope = 3.39 and intercept = 25. For the Ektachem Amylase method the reaction-rate ratio between salivary and pancreatic amylase was calculated to be 0.89, relative to that of the Phadebas Blue Starch method. A calibration value for the Nordic Amylase Calibrator to be used on Ektachem analysers was determined to be close to 469 U l-1 for the current batch. However, since the difference from the stated value of 460 U l-1 is negligible, the authors recommend the use of the stated value for this and future batches of the Nordic Amylase Calibrator. An error of around 10% introduced by the presence of salivary amylase is comparable to the methods accepted by the Scandinavian Committee on Enzymes. Introduction of a consensus calibration reduced the interlaboratory variation by up to 40% at all levels.

Dry Reagent Technology. Kodak Ektachem 700 XR in Clinical Enzymology

The comparability of results for enzyme activity concentrations estimated with the methods recommended by the Scandinavian Committee on Enzymes(SCE) or the subcommittee on Enzymes of the European Committee for Clinical Laboratory Standards(ECCLS), and with the Kodak Ektachem methods, are discussed. As the Ektachem system in principle uses the IFCC methods at 37 degrees C as a reference, the results compare reasonably well for the alanine amino-transferase(ALAT), aspartate aminotransferase(ASAT), creatine kinase(CK) and gamma-glutamyltransferase(GT). The Ektachem reference method for lactate dehydrogenase(LD) is in principle the SCE method. The reasons for lower values with the SCE method are discussed. The interference on the Ektachem alkaline phosphatase (ALP) method from high concentrations of methotrexate(MTX) in serum, is shown. Results from our investigations on the interference by heparin in enzyme determinations on Ektachem are given. The problems with CK determinations in cancer patients regarding myocardial diseases are well known. When CK-BB is present in serum, the CK-B concentration is apparently lower using the Ektachem CK method than with use of the CK-MB slide, probably relating to the fact that chelator is omitted from the CK slide, while EGTA is supplied in the CK-MB slide. The user's dependence on the manufacturer for the choice of methods and the quality of the reagents, makes it important for laboratories and the Kodak Company to collaborate with the intention to continuously improve the Ektachem methodologies. The future possibilities of this technology seem to be nearly unlimited.

Recommendation for collection of venous blood from children, with special reference to production reference values

Reference values should be produced under standardized conditions. To enable comparison it is desirable to use the same procedure also in other clinical situations. A procedure for the collection of venous blood from children with special reference to production of reference values is recommended. It deals with five items: preparation of the child before specimen collection, preparation of the blood collection site, equipment for specimen collection, the specimen collection itself, and handling and storage of the specimen. Alternative methods are described since no single method is suitable for all paediatric age groups. The problem of adhering to a proposed procedure during routine clinical work is also commented upon. The recommendation has been produced as a joint effort of the Scandinavian Committee on Reference Values and a working group set up by the National Paediatric Societies in the Nordic countries.

The Diagnostic accuracy of three recommended methods for serum aspartate aminotransferase assays in patients suspected of myocardial infarction and hepatobiliary diseases

Serum aspartate aminotransferase (AST) activity was measured by the methods recommended by the Scandinavian Committee on Enzymes (SCE) and by the International Federation of Clinical Chemistry (IFCC) with pyridoxal phosphate (PLP) and without (-PLP) in one laboratory at 37 degrees C with the Abbott ABA-100 and in another at 30 degrees C with the IL Multistat III. Reference ranges were determined on 195 healthy hospital staff. Sera from 102 patients with suspected hepatobiliary disease (HBD) and 104 with suspected myocardial infarction (MI) were assayed at both laboratories by all three methods. Based on the above reference ranges, all assays with each method at both hospitals were abnormal in 59 of 67 cases with HBD and 53 of 55 with MI. In aggregate, all three methods yielded comparable rates of misclassification (20-23). The SCE method gave highest false negatives (18) and lowest false positives (5); the IFCC method gave lowest false negatives (1) and highest false positives (20); intermediate values of 8 false positives and 12 false negatives were given by the IFCC (-PLP) method. Using receiver operating characteristic (ROC) curves, the SCE method was clearly superior at 30 degrees C, and the IFCC (-PLP) method was marginally superior at 37 degrees C. However, when the decision threshold corresponded with a 2.5% false positive rate in the non-HBD, non-MI patients, the SCE method gave the lowest false negatives at both temperatures and, on the basis of the present data, must be considered to be the method of choice for AST activity determinations.

Evaluation of commercially formulated aspartate aminotransferase and alanine aminotransferase activity determinations by the scandinavian committee on enzymes and IFCC methods as modified for use with automated enzyme analysers

The performance characteristics of the Scandinavian Committee on Enzymes (SCE) methods for the assay of aspartate aminotransferase (AST) and alanine aminotransferase (ALT) were determined using six automated enzyme analysers. The reagent formulation did not include pyridoxal phosphate (PLP). An optimal operating mode was defined for each instrument and precision was assessed in greater detail on four instruments. A points rating system was devised to place the instruments in the following order of proficiency: IL Multistat III, LKB-8600, Gilford 3500, ABA 100. In contrast to AST, the ALT activity of patient samples was unstable at -20 degrees C over periods as short as seven days. The performance characteristics of the IFCC methods for assay of AST and ALT activities were determined by using three automated enzyme analyzers in order to assess the effect of PLP upon precision and activity of four quality control sera, and to compare the SCE and IFCC methods. Precision of AST assays did not alter on omission of PLP from the IFCC formulation, while that of ALT assays showed slight deterioration. The decrease in activity on omitting PLP was variable with each instrument. A points-rating system was devised to place the methods in the following order of precision: AST: IFCC (-PLP) 118, IFCC 109, SCE 61; ALT: IFCC 125, IFCC (-PLP) 97, SCE 66. The IFCC methods offer better precision, and the overall change on omitting PLP is minimal.

SCE Nordic alpha-amylase study. II: Assessment of proposed calibration procedure. A report by the Scandinavian Committee on Enzymes (SCE).

Eighty-seven Nordic Hospital laboratories participated in a joint SCE-NORDKEM follow-up study of the long-term stability of the previously established calibration factors for a number of alpha-amylase routine methods based on six different substrates. Human control materials with 90% pancreatic, 90% salivary, and pure pancreatic alpha-amylases were measured by the participants. The data were plotted before and after calibration of each method using a human pancreatic calibrator with an assigned catalytic concentration of 390 U/l (Phadebas blue starch method, 37 degrees C). As in the previous study, carried out 9 months earlier, the pre-calibration values varied over a six-fold range. The post-calibration values of all methods except those based on a tetraose substrate showed an acceptable inter-laboratory comparability. As a temporary measure, SCE recommends that the Nordic laboratories calibrate the accepted routine methods by their individual calibration factor. Detailed suggestions for calibration procedures and a discussion of the principles of transferability will shortly be published by the SCE in this journal.

Will implementation of ICES delay method standardization in clinical enzymology? Scandinavian Committee on Enzymes.

Will implementation of ICES delay method standardization in clinical enzymology? Scandinavian Committee on Enzymes.

The Microfilmed Collections of Russian Archival Materials in the Danish and Swedish National Archives

The national archives of Denmark and Sweden have engaged Soviet archives in extensive and probably unique exchanges of copied materials. These two archives consequently hold substantial quantities of Soviet archival records, records sometimes of extraordinary value, which in some cases are scarcely accessible in any other part of the world, including the Soviet Union. Approximately 40 percent of the holdings of Soviet documents in the Danish National Archive come from the Arkhiv vneshnei politiki Rossii. The fact that it is very difficult to gain access to this institution considerably enhances their importance. The Swedish holdings are similar.The Russian documents in both archives were acquired in two phases, and phase one was common to both. In 1928, archivists and historians from Denmark, Norway, and Sweden formed a joint Scandinavian committee for the exploration of the Russian state archives (Den Nordiske Faelleskomite for Udforskning af de russiske Statsarkiver).

Serum LD-1 activity in suspected acute myocardial infarction.

We have studied the diagnostic value of measuring lactate dehydrogenase (LD) isoenzyme 1 in serum of 331 cases of suspected acute myocardial infarction (AMI). At a discriminatory level of 200 U/L (Scandinavian Committee on Enzymes, recommended method for the determination of LD) LD 1 verified the diagnosis in 96% of the AMI cases and excluded it in 96% of the not-AMI cases when samples were drawn 24-72 h after onset of pain. The correlation between 24-h S-LD-1 and 16-h S-CK B activities was 0.94 in the AMI cases. We found that quantitation of serum LD-1 is diagnostically more reliable than the serum LD-1/LD ratio.

Serum ASAT, ALAT, ALP, LD, GT, and CK determined in the Cobas-Bio centrifugal analyser by the methods of the Scandinavian Committee on Enzymes

The recommended methods of the Scandinavian Committee on Enzymes [4, 5, 6, 7, 8] have been applied to the Cobas-Bio centrifugal analyser. Reagents and serum volumes were scaled down and final molarities were kept equal. Serum volumes in microliters were as follows: ASAT 30, ALAT 30, ALP 3, LD 5, GT 20, and CK 10. Including the dead space of the sample cup, the volume needed to perform all six tests was 113 microliter. Within-run and between-run precision (CV%) were as follows: ASAT 1.32 and 1.95, ALAT 1.68 and 2.93, ALP 1.56 and 3.10, LD 1.63 and 4.44, GT 0.81 and 2.23, and CK 1.02 and 1.94. Mean deviations (%) from target values of two commercial sera were as follows: ASAT -0.3 and -0.4, ALAT -0.4 and -2.2, ALP -1.8 and -7.3, LD 0.4 and -6.2, GT 13.9 and -10.7, and CK -4.9 and -1.3. Results of all the methods correlated well with those obtained with their respective manual methods. Analytical time for 28 samples of each analyte was 10 min, apart from CK which was 14 min. Reagent cost per sample was 0.6, 0.9, 0.1, 0.3, 0.9, and 26 US cents respectively. All reagents were prepared in the laboratory, except those for CK which were bought from J.T. Baker (Phillipsburgh, NJ, USA). In conclusion, the methods keep the features of the manual methods but they are more precise and practicable, much faster and cheaper, and use minimal amounts of sera more convenient for paediatric work.

On the transportability of linear discriminant functions.

Different methods can give different results for the same analyte, and inconsistent answers may be obtained if such results are used in linear discriminant functions. This is an important factor to consider when transporting linear discriminant functions from one laboratory to another; the example of alkaline phosphatase activity and the differential diagnosis of hypercalcaemia has recently been given. This study shows that results obtained by the method recommended by the Scandinavian Committee on Enzymes for alkaline phosphatase may be used in the calculation of the discriminant functions used for the differential diagnosis of hypercalcaemia and considers other factors that may affect the discrimination. It is concluded that, with care, linear discriminant functions may be transported from one laboratory to another.

Serum ASAT, ALAT, ALP, LD, GT, and CK determined in the Cobas-Bio centrifugal analyser by the methods of the Scandinavian Committee on Enzymes

Serum ASAT, ALAT, ALP, LD, GT, and CK determined in the Cobas-Bio centrifugal analyser by the methods of the Scandinavian Committee on Enzymes

Effects of posture on concentrations of blood constituents in healthy adults: practical application of blood specimen collection procedures recommended by the Scandinavian Committee on Reference Values.

Different procedures for the collection of blood for the determination of reference values in healthy adults have been subjected to practical testing. The Scandinavian Committee on Reference Values suggested that subjects lying in bed after an overnight sleep and ambulatory individuals, after 15 min of sitting in a chair, were two suitable and different reference populations. In forty subjects we found an increase from lying to sitting position of about 6.5% in the serum concentrations of proteins, enzymes and lipids. The corresponding increases for S-calcium and B-haemoglobin were approximately 3% whereas S-thyroxine, unexpectedly, changed by 11%. There were no significant changes of potassium and sodium values. For some constituents the changes were age and sex-dependent being greater in a group of elderly women as compared to a group of younger men. After 1 h of recumbency the concentrations of the constituents generally returned to those in the initial, lying position.

Turbidity as a cause of error in the L-alanine transferase (ALAT) method.

When performing the ALAT-determination as recommended by the Scandinavian Committee on Enzymes, turbidity will develop due to a low ionic strength of the buffer. At the end of the pre-incubation period, the turbidity may still be developing, increasing the absorbance and lowering the ALAT-activity by 0-5 U/l. Turbidity and the error introduced in the assay, can be eliminated by increasing the ionic strength of the buffer by addition of NaCl.

Reference values for six enzymes in plasma from newborns and women at delivery

We have determined the distribution in cord blood from healthy newborns of six enzymes: creatine kinase, lactate dehydrogenase, aspartate and alanine aminotransferase, alkaline phosphatase and γ-glutamyltransferase. The concentration of enzymes were determined according to the methods recommended by the Scandinavian Committee on Enzymes. The distribution of isoenzymes and of enzymes in blood from women at delivery was investigated also. All distributions were positively skewed. The upper reference limits of cord blood exceeded those found in mother blood by a factor of eight for γ-glutamyltransferase, and for lactate dehydrogenase and creatine kinase by a factor of two.

A comparison of reaction conditions for the automated determination of γ-glutamyltransferase activity in serum

The methods of Rosalki and Tarlow and the Scandinavian Committee on Enzymes for the determination of γ-glutamyltransferase activity in serum have been compared, with an automatic reaction-rate analyzer in which the reaction is initiated by the addition of a concentrated solution of γ-glutamyl-p-nitroanilide. Results are approximately 4% lower by the Scandinavian method, because of its lower substrate concentration. However, both methods are of comparable reproducibility. The greater stability of the more dilute substrate solution specified in the Scandinavian method has been confirmed, but attempts to stabilize solutions of γ-glutamyl- P-nitroanilide at the higher concentrations recommended by Rosalki and Tarlow by the addition of organic solvents were accompanied by some enzyme inhibition. The comparative instability of the substrate solution of Rosalki and Tarlow is unlikely to lead to erroneous results; however, the Scandinavian formulation offers the advantage of a more economical use of reagents, at the expense of a small and probably unimportant reduction in sensitivity.

Reference values for six enzymes in plasma from newborns and women at delivery.

We have determined the distribution in cord blood from healthy newborns of six enzymes: creatine kinase, lactate dehydrogenase, aspartate and alanine aminotransferase, alkaline phosphatase and gamma-glutamyltransferase. The concentration of enzymes were determined according to the methods recommended by the Scandinavian Committee on Enzymes. The distribution of isoenzymes and of enzymes in blood from women at delivery was investigated also. All distributions were positively skewed. The upper reference limits of cord blood exceeded those found in mother blood by a factor of eight for gamma-glutamyltransferase, and for lactate dehydrogenase and creatine kinase by a factor of two.

EDTA effect on creatine kinase (CK) and on the SCE reagent.

The inclusion of EDTA in the creatine kinase reagent recommended by the Scandinavian Committee on Enzymes was shown to increase reagent stability from less than 24 h to 5 days. Part of this effect can be explained by the fact that EDTA delays the formation of inhibitory products formed when N-acetyl cysteine is oxidized. The addition of EDTA to the reagent also results in increased measured CK activity. This effect is more pronounced for CK-BB than for CK-MM. Calcium and ferric ions are shown to inhibit the enzyme and the chelation of these ions can partly explain the observed increase of CK acitivity.

Creatine kinase B-subunit activity in human serum. I. Development of an immunoinhibition method for routine determination of S-creatine kinase B-sununit activity

The properties of an inhibiting antibody directed against the M-subunits of human creatine kinase (EC 2.7.3.2, CK) were investigated in the reaction system recommended by the Scandinavian Committee on Enzymes (S.C.E.). At 37° C the rate of immunoinhibition of human CK M-subunit dependent activity corresponded to a t 1 2 of 38 s giving a k value of −2 per cent · s −1 when samples were incubated in the S.K.E. CK reagent A in the presence of antibody. Under the selected conditions immunoinhibition of S-CK M-subunit activity up to 1800 U/l was 99 per cent completed within 5 minutes using undiluted samples. No inhibition of CK B-subunit activity occurred at the chosen concentration of antibody. The inhibition data were verified using human sera and electrophoretically homogeneous preparations of human CK isoenzymes BB and MM. Sample adenylate kinase (EC 2.7.4.3, AK) was found to constitute a potential source of falsely increased S-CK B activity. As reported in the accompanying paper a S-CK B value of 15 U/l was used as a discrimination value in the diagnosis of acute myocardial infarction. The S.C.E. CK method incorporates a combination of two AK inhibitors adenosine 5'-monophosphate and P 1, P 5-diadenosine 5'-pentaphosphate. However, a frequency analysis of sample AK activities demonstrated that AK activities of more than 8 U/l will occur in about 10 per cent of the cases. Consequently, it was deemed necessary to measure the individual sample blank AK rates. The routine procedure developed thus included three separate measurements: determination of total S-CK and of S-CK B activities in the absence and presence of antibody, respectively. As the immunoinhibition was only 99 per cent complete a value corresponding to one per cent of the total S-CK activity was subtracted from the measured S-CK B activity. Likewise, the individual sample AK activity had to be measured and subtracted from the apparent S-CK B activity. The within-series precision of this S-CK B method at the levels of 10 U/l and 20 U/l corresponded to C.V. values of 10 and 5 per cent, respectively. Day-to-day precision at the level of 417 U/l corresponded to a C.V. of 4 per cent. The day-to-day precision of a control, total CK activity 625 U/l, gave a mean value of 53% ± 3% of CK B activity.