{"title":"On the biocompatibility of IBM 2997 continuous flow plateletapheresis.","authors":"J Lindena, H Burkhardt, H M Aulmann","doi":"10.1515/cclm.1990.28.7.465","DOIUrl":"https://doi.org/10.1515/cclm.1990.28.7.465","url":null,"abstract":"<p><p>During the procedure of centrifugation cytapheresis donors occasionally experience adverse clinical reactions. We evaluated the possibility of whether activation of granulocytes and their subsequent release reactions, which may have been triggered by this extracorporeal circuit, were responsible for these adverse effects. Six blood samples were obtained during various set intervals during plateletapheresis. Of these, four samples were taken directly from each donor. The remaining two were drawn from the efferent lines, i.e. those which return blood from the cytapheresis machine back to the donor. Reactive oxygen species produced by granulocytes were monitored by chemiluminescence using microamounts of whole blood or isolated granulocytes. Furthermore, secreted granulocyte products such as neutral proteinase elastase, present in plasma in a complex with alpha 1-proteinase inhibitor (complexed elastase), and lysosomal beta-glucuronidase were examined. A complete blood cell count, as well as values of haemoglobin, haematocrit, lactate dehydrogenase, protein, albumin and proteinase inhibitors such as alpha 2-macroglobulin and alpha 1-proteinase inhibitor were also determined. Complexed elastase increased from a preapheresis value of about 140 micrograms/l to about 180 micrograms/l at the end of the cytapheresis. All other clinical chemical and cytological values were 8 to 12 percent lower than preapheresis values, which can be attributed to inherent plasma volume expansion. Reduced chemiluminescence was observed upon stimulation of phagocytes in the whole blood assay (about 700 counts/min x 10(3) x 50,000 cells vs. about 600 counts/min x 10(3) x 50,000 cells). This decrease was also seen with stimulated granulocytes (about 5800 counts/min x 10(3) x 50,000 cells vs. about 4500 counts/min x 10(3) x 50,000 cells.(ABSTRACT TRUNCATED AT 250 WORDS)</p>","PeriodicalId":15649,"journal":{"name":"Journal of clinical chemistry and clinical biochemistry. Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"28 7","pages":"465-70"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/cclm.1990.28.7.465","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12864550","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
A Hadberg, C Hassager, P Hildebrandt, C Christiansen
{"title":"Comparison of two immunoinhibitory methods with agarose gel-electrophoresis for measuring the MB isoenzyme of creatine kinase in serum from cases of suspected myocardial infarction.","authors":"A Hadberg, C Hassager, P Hildebrandt, C Christiansen","doi":"10.1515/cclm.1990.28.7.453","DOIUrl":"https://doi.org/10.1515/cclm.1990.28.7.453","url":null,"abstract":"<p><p>Two immunoinhibitory methods for measuring creatine kinase-MB (a dry chemical and a wet chemical method) were compared with the commonly used agarose gel electrophoretic method, using 563 serum samples from 235 patients with suspected acute myocardial infarction. Comparison of the electrophoretic and the dry chemistry methods showed the linear relationship: electrophoretic method = -6.5 U/l + 1.22 x dry chemistry method, r = 0.943. For the wet chemistry method the relationship was: electrophoretic method = -7.2 U/l + 1.19 x wet chemistry method, r = 0.854. Parallel determinations of total creatine kinase were also done and the methods were virtually identical in performance. Compared with the electrophoretic method (which showed a 15% prevalence of acute myocardial infarction), these classifications showed sensitivities of 0.92 and 0.67 and specificities of 0.94 and 0.99 (dry and wet chemistry, respectively; using methods recommended by the manufacturers). After optimization of discriminators the sensitivity was increased to 0.94/0.92 and the specificity to 0.99/0.99.</p>","PeriodicalId":15649,"journal":{"name":"Journal of clinical chemistry and clinical biochemistry. Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"28 7","pages":"453-8"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/cclm.1990.28.7.453","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13381683","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
J P Braun, G Ouedraogo, B Thorel, C Médaille, A G Rico
{"title":"Determination of plasma alpha-amylase in the dog: a test of the specificity of new methods.","authors":"J P Braun, G Ouedraogo, B Thorel, C Médaille, A G Rico","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Commercially available chromogenic substrates for the assay of alpha-amylase were tested for specificity in dog plasma. Blocked alpha-4-nitrophenylmaltoheptaoside and non-blocked beta-4-nitrophenylmaltoheptaoside showed no interference with glucoamylase and were suitable for the measurement of alpha-amylase in dog plasma. In contrast, an alpha-4-nitrophenylmaltoheptaoside showed interference, and was therefore an inappropriate substrate. Reference values with the blocked substrate in a group of 82 non-selected 3 month- to 10 year-old male and female dogs were 355 +/- 131 U/l (mean +/- standard deviation) at 30 degrees C.</p>","PeriodicalId":15649,"journal":{"name":"Journal of clinical chemistry and clinical biochemistry. Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"28 7","pages":"493-5"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13381689","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Thrombocytes as interfering factors in clinical chemistry.","authors":"W G Guder","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":15649,"journal":{"name":"Journal of clinical chemistry and clinical biochemistry. Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"28 7","pages":"445"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13381681","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
M F van Ginkel, G B van der Voet, H G van Eijk, F A de Wolff
{"title":"Aluminium binding to serum constituents: a role for transferrin and for citrate.","authors":"M F van Ginkel, G B van der Voet, H G van Eijk, F A de Wolff","doi":"10.1515/cclm.1990.28.7.459","DOIUrl":"https://doi.org/10.1515/cclm.1990.28.7.459","url":null,"abstract":"<p><p>The binding of aluminium in rat serum was studied. Rats were loaded intraperitoneally with different doses of aluminium(III)chloride 4 times during one week, before being killed by cardiac puncture. One ml of serum was applied to a Sephacryl S-200 SF column and 70 fractions were collected. In the collected fractions, the distribution of aluminium was measured and compared with the concentrations of total protein, transferrin, and citrate. The presence of a high molecular weight aluminium-complex in serum is confirmed. Although a possible role for albumin cannot be excluded, it is most likely that transferrin plays a role as a carrier for biological transport of aluminium in plasma. In addition to transferrin, aluminium was shown to be associated with citrate in serum, resulting in a low-molecular weight complex. It is postulated that citrate acts as a chelator for aluminium, and that the Al/citrate complex in serum may play an important role in intracellular accumulation, and hence the toxicity, of aluminium.</p>","PeriodicalId":15649,"journal":{"name":"Journal of clinical chemistry and clinical biochemistry. Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"28 7","pages":"459-63"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/cclm.1990.28.7.459","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13381684","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
C Farace, B Blanchot, D Champiat, P Couble, G Declercq, J L Millet
{"title":"Synthesis and characterization of a new substrate of Photinus pyralis luciferase: 4-methyl-D-luciferin.","authors":"C Farace, B Blanchot, D Champiat, P Couble, G Declercq, J L Millet","doi":"10.1515/cclm.1990.28.7.471","DOIUrl":"https://doi.org/10.1515/cclm.1990.28.7.471","url":null,"abstract":"<p><p>A derivative of luciferin, 4-methyl-D-luciferin, was synthesized in low yield, and characterized by its ultraviolet and fluorescence spectra. The spectra of luciferin and its derivative are very similar. 4-Methyl-D-luciferin is a substrate of Photinus pyralis luciferase, and it causes light emission in luminometric assays.</p>","PeriodicalId":15649,"journal":{"name":"Journal of clinical chemistry and clinical biochemistry. Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"28 7","pages":"471-4"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/cclm.1990.28.7.471","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13381685","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Measurement of serum alcohol dehydrogenase activity at different pH-values during the course of viral hepatitis in children.","authors":"A A Elghaffar, L Chrostek, M Szmitkowski","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Serum alcohol dehydrogenase activity was estimated at pH 10.4 (optimum for the typical liver isoenzyme), 8.8 (optimum for atypical liver isoenzyme), at the physiological serum pH of 7.4, and at pH 9.2, with a view to obtaining the greatest possible difference between patients and controls. Measurements were performed on the sera of 39 children aged from 2 to 13 years, using the Technicon analyzer RA-1000 with the continuously measuring method of Bonnichsen & Brink. Blood sera were tested at the onset of viral hepatitis, in the first week of hospitalization, and three times thereafter at intervals of 7 to 9 days. During the illness, the activity of serum alcohol dehydrogenase, measured at different pH-values, was higher than that of controls. The ratio of activity at pH 10.4 to activity at pH 8.8 in the sera differed from that previously reported for liver cells. The highest increase in alcohol dehydrogenase activity was at pH 9.2. The diagnostic sensitivity of alcohol dehydrogenase determination at this pH is lower than that of alanine aminotransferase, gamma-glutamyltransferase and aspartate amino-transferase, but higher than that of lactate dehydrogenase, alkaline phosphatase and bilirubin; alcohol dehydrogenase activity also shows the best correlation with the activity of gamma-glutamyltransferase.</p>","PeriodicalId":15649,"journal":{"name":"Journal of clinical chemistry and clinical biochemistry. Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"28 7","pages":"497-9"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13381690","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"A comparison of four immunometric assays for myeloperoxidase using luminescent and colorimetric signal detection.","authors":"I Janda, H Jaensch, J Braun, W G Wood","doi":"10.1515/cclm.1990.28.7.475","DOIUrl":"https://doi.org/10.1515/cclm.1990.28.7.475","url":null,"abstract":"<p><p>This communication presents four different assay systems for the determination of myeloperoxidase in body fluids. One is based on conventional chemiluminescence, two on luminescence-amplified enzyme measurement using either spiroadamantane-1,2-dioxetanes with alkaline phosphatase or luminol/peroxidase/4-iodophenol coupled with a peroxidase label. The assays covered the range 0-600 micrograms/l peroxidase. Established reference range for EDTA plasma from healthy volunteers gave an upper limit of 250 micrograms/l (95% confidence limits). Intra-assay coefficients of variation were less than 5% for all assays, as seen in compound precision profiles. Inter-assay variation was less than 10% throughout the whole concentration range. Kinetic curves for the light production were performed over a 2 hour period for the enhanced luminescence assays. Dynamic ranges of these assays were compared with the conventional colorimetric assay using 4-nitrophenyl phosphate--alkaline phosphatase. The assay was standardized using a commercially available myeloperoxidase preparation with defined enzymatic activity. The protein content was estimated and the laboratory standard compared and calibrated in mass units.</p>","PeriodicalId":15649,"journal":{"name":"Journal of clinical chemistry and clinical biochemistry. Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"28 7","pages":"475-80"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/cclm.1990.28.7.475","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13325225","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Spiroadamantane dioxetane substrates--stable labels for luminescence-enhanced enzyme immunoassays.","authors":"W G Wood","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>This short communication describes the use of spiroadamantane-1,2 dioxetane substrates for alkaline phosphatase and beta-D-galactosidase in the development of luminescence-enhanced enzyme immunoassays. Until the present work, only peroxidase-luminol/peroxidase systems had been used in such assays. The light reaction kinetics were studied from the time of initiation of the light reaction up to 2 days later. The methods is illustrated by the determination of myeloperoxidase, based on microtitre plate technology, coupled with a microtitre plate luminometer which needs no injector. The alkaline phosphatase and peroxidase systems were compared.</p>","PeriodicalId":15649,"journal":{"name":"Journal of clinical chemistry and clinical biochemistry. Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"28 7","pages":"481-3"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13381686","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
M P Panozzo, D Basso, C Fabris, D Faggian, T Meggiato, M Plebani, G Del Favero, P Fogar, P Scalon, C Ferrara
{"title":"Diagnostic utility of a new monoclonal antibody pancreatic isoamylase assay in chronic pancreatic diseases.","authors":"M P Panozzo, D Basso, C Fabris, D Faggian, T Meggiato, M Plebani, G Del Favero, P Fogar, P Scalon, C Ferrara","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>In order to evaluate the efficacy of a monoclonal pancreatic (P) isoamylase assay in the diagnosis of chronic pancreatic disease and to compare the behavior of this test with that of amylase and elastase 1, these three enzymes were measured in the sera of 39 healthy controls, 28 patients with pancreatic cancer, 50 with chronic pancreatitis and 60 with extra-pancreatic diseases. In patients with chronic relapsing pancreatitis, increased P-isoamylase and elastase 1 values were found in similar percentages (about 70%), whereas the percentage for elevated amylase values was lower (52%). Elastase 1 was increased in 52% of patients with pancreatic cancer, while the other two enzymes were only occasionally elevated. The levels for all three enzymes were abnormal in some patients with extra-pancreatic diseases. It may be concluded that this assay for P-isoamylase determination is sufficiently sensitive and reliable in detecting pancreatic inflammation, even though some limitations concerning its specificity should be born in mind.</p>","PeriodicalId":15649,"journal":{"name":"Journal of clinical chemistry and clinical biochemistry. Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"28 7","pages":"485-8"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13381687","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}