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Biomedical subjects

U B Seiffert

Publications and source records attributed to U B Seiffert.

At least 19 recordsLinked to original sources
PubMed1996

Computer assisted interpretation of laboratory test data with 'MDI-LabLink'.

Physicians have to confront an enormous output of laboratory data. Normally, only a few experts manually perform the interpretation of highly specialised laboratory tests. PC Windows based 'MDI-LabLink' automates interpretation and expands traditional rule-based expert systems with flexibility and graphic illustrations of complex laboratory data. The laboratory can adjust the interpretation database to its specific needs, maintaining full control over program output. The structured input that 'MDI-LabLink' requires, supports dynamic test scheduling. It can be used to train personnel in the interpretation of laboratory test results. The program provides the clinician with a report that visualises the defect of the evaluated organ system with bitmap pictures and 3-dimensional graphics. Patient follow-ups present in tabular and graphical form. Changes in the severity of the pathobiochemical defect, induced, for example, by therapy, are monitored automatically. Applications available include interpretations of isoenzyme patterns, diagnosis of urinary proteinuria and cerebrospinal fluid analysis.

Chemistry, Clinical↗
PubMed1996

Physical activity releases prostate-specific antigen (PSA) from the prostate gland into blood and increases serum PSA concentrations.

Determination of prostate-specific antigen (PSA) is an established tool in detecting prostate cancer. However, the effect of physical activity on the PSA concentration in serum is controversial. We measured serum concentrations of PSA and prostatic acid phosphatase (PAP) in 301 healthy outpatients before and after they performed standardized exercise. Immediately after 15 min of exercise on a bicycle ergometer, their serum PSA concentrations increased by as much as threefold. The increase was age dependent and correlated to the PSA concentration before exercise. This increase was evident in both the free and complexed fractions of PSA. The amount of PSA secreted into blood depends on the volume of the prostate, whereas productivity of the prostate epithelium remains constant or increases slightly with age. We present cutoff values for clinical use. PAP was also increased, but to a lesser extent. The PSA and PAP secretion mechanisms differ. Our data suggest that extensive physical activity should be avoided before blood sampling for diagnostic purposes and, in case of an increase, the PSA concentration should be controlled after an exercise test.

Acid Phosphatase↗
PubMed1995

[Cyfra 21-1--a new tumor marker of the cytokeratin series in differential diagnosis of lung diseases].

BACKGROUND: Cyfra 21-1 is a novel marker for non small cell lung cancer. Up to now only few data about the value of Cyfra 21-1 in the diagnosis of malignant and non-malignant pulmonary diseases are available. Further the effect of long-time cigarette consumption on serum concentrations of Cyfra 21-1 has not been described. Aim of this study therefore was the determination of Cyfra 21-1 in different malignant and non-malignant pulmonary diseases and in healthy smokers and nonsmokers. PATIENTS: Sera of healthy individuals (control group, n = 121; 63 smokers and 58 nonsmokers), patients with chronic bronchitis (n = 50), lung fibrosis (n = 38), exogen allergic alveolitis (n = 32), lung tuberculosis (n = 45), sarcoidosis (n = 30), small cell lung cancer (n = 60), squamous cell carcinoma (n = 53), non-small cell carcinoma (n = 29) and adenocarcinoma (n = 52) were analyzed. RESULTS: Within the control group no significant differences of the Cyfra 21-1 serum concentration were observed between smokers and nonsmokers. Serum concentrations of Cyfra 21-1 were similar in the control group, patients with non-malignant pulmonary diseases and patients with small cell lung cancer whereas serum concentrations were significantly increased in patients with non-small cell lung cancer, adenocarcinoma and squamous cell carcinoma. CONCLUSIONS: The data confirm the high sensitivity and specific of Cyfra 21-1 for the differential diagnosis between malignant and non-malignant pulmonary diseases as well as small cell and non-small cell lung cancer.

Adolescent↗
PubMed1993

Cyclosporin treatment in rheumatoid arthritis is associated with an increased serum activity of beta-glucuronidase.

The serum activity of beta-glucuronidase (beta-gluc) has been presumed to indicate the disease activity in rheumatoid arthritis (RA). In 10 patients with RA the serum beta-gluc was repeatedly determined after the initiation of a treatment with cyclosporin for one year. A significant increase of beta-gluc was found after 8, 12 and 16 weeks compared to the values before treatment, while the concentration of the soluble interleukin 2-receptor decreased. The data reveal, that beta-gluc is not a useful indicator of the disease activity during cyclosporin treatment.

Arthritis, Rheumatoid↗
PubMed1993

Fast lipoprotein chromatography: new method of analysis for plasma lipoproteins.

Fast lipoprotein chromatography (FLPC) is a novel method for quantifying lipoproteins. Plasma proteins are separated by fast-flow gel filtration. Lipoproteins are detected by post-column derivatization with an enzymatic cholesterol reagent. FLPC resolves very-low-, low-, and high-density lipoproteins (VLDL, LDL, and HDL, respectively) and completely separates apolipoprotein Al- and apolipoprotein B-containing lipoproteins. CVs for VLDL-cholesterol, LDL-cholesterol, and HDL-cholesterol are 5.8%, 2.0%, and 1.9%, respectively. We compared FLPC with a combined ultracentrifugation and precipitation method and obtained correlation of r = 0.979, 0.978, and 0.933 for VLDL-cholesterol, LDL-cholesterol, and HDL-cholesterol, respectively. Triglyceride concentrations up to 9.00 g/L did not interfere with the quantification of lipoproteins by FLPC. We conclude that FLPC is a precise and reliable method for the analysis of plasma lipoproteins that complements conventional techniques.

Apolipoprotein A-I↗
PubMed1990

[Determination of glycosylated hemoglobin using affinity chromatography. A comparison of methods].

The determination of glycated hemoglobin is used to judge the quality of adjustment in diabetic diagnostics as this value best represents the mean concentration of blood glucose of recent weeks. At the moment several methods for the determination of glycated hemoglobin are available. A new method is the microcolumn affinity chromatography which proved to be very practicable in our investigations. This paper presents results concerning precision, correlations with other methods, possible interferences and concordance.

Chromatography, Affinity↗
PubMed1990

[Fructosamine as a diagnostic parameter in the clinical routine].

The fructosamine normal range was established from a collective of 90 healthy individuals as 219-285 mumol/l (+/- 2s; mean 240 mumol/l). From a group of 10 diabetics day profiles of glucose, protein, albumin, and fructosamine were recorded by measuring these parameters three times per day at 8.00, 11.30, and 15.00. The fructosamine concentration was essentially constant also when related to protein or albumin. Fructosamine, HbAlc, CK, and CK-MB were determined from 12 diabetics with fresh myocard infarct (7 diabetics, 5 non-diabetics). Surprisingly, diabetics as well as non-diabetics manifested high fructosamine concentrations. The origin of the fructosamine increase with non-diabetic myocard infarct patients is not yet known. Possibly the acute metabolic disorder plays an important role. An influence of fibrinogen on fructosamine is also conceivable. Additional investigations, including therapy of lysis, will be carried on. The stability of the fructosamine was examined by storing 50 sera (fructosamine 295-491 mumol/l, glucose 180-279 mg/dl) at different temperatures (+ 25 degrees C, + 4 degrees C, - 20 degrees C). At - 20 degrees C and + 4 degrees C fructosamine increases by up to 2% in 24 hours. At + 25 degrees C a 6% increase in fructosamine was observed within the same observation period.

Blood Proteins↗
PubMed1989

Endoprotease in human liver transforming multiple forms of alkaline phosphatase.

Two forms of alkaline phosphatase, extracted from human liver and named API1 and API3, are of high molecular mass, but API3 is the larger molecule and is membrane-bound while API1 is smaller and soluble. Enzyme kinetics are identical. It is suggested that API1 is produced from API3 by an endoprotease. We demonstrated the action of an endoprotease in human liver homogenate converting API3 into API1. In the absence of this enzyme no conversion occurred. This enzyme is active at an acidic pH (less than 6.5) in the presence of Ca.. or Mg.. -ions. It is inhibited by traces of EDTA. It is insensitive to diisopropyl fluoro-phosphate, to leupeptin and to reducing or oxidizing chemicals. At alkaline pH (8.6) its activity is rapidly destroyed. The enzyme is stable in acidic buffer. We conclude that API1 is indeed formed from API3 in the living cell by enzymatic conversion.

Alkaline Phosphatase↗
PubMed1989

Alkaline phosphatase isoenzymes in rheumatic diseases.

Serum alkaline phosphatase isoenzymes were determined quantitatively by electrophoresis on cellulose acetate in 168 patients with rheumatic diseases subgrouped for disease activity. Median values of total alkaline phosphatase and bone isoenzyme activity, as well as frequency of patients showing pathological values, increased gradually and significantly corresponding to disease activity in rheumatoid arthritis and ankylosing spondylitis, from 0% in inactive to 90% in very active forms. Bone isoenzyme was much more sensitive than total alkaline phosphatase in moderate disease activity and was also correlated to the number of involved extravertebral joints and pain in ankylosing spondylitis. No correlation was found with stage or duration of disease, age, sex, and erythrocyte sedimentation rate. Additional to bone isoenzyme, liver isoenzymes were elevated in some patients, but with only a weak correlation with disease activity. The intestinal isoenzymes were always normal. We conclude that quantitative determination of serum alkaline phosphatase bone isoenzyme activity is a major indicator for the assessment of disease activity and therapeutic monitoring in rheumatoid arthritis and ankylosing spondylitis.

Alkaline Phosphatase↗
PubMed1988

Automated determination of serum (plasma) and urine iron: a comparative investigation of chromogens improved tripyridyltriazine micromethod.

Four different, well known colour reagents for iron determination were tested in a citrate buffer at pH 2.0 under the same automated standard conditions and compared with a manual reference method on human serum and plasma samples. Specific results were obtained only with the chromogen tripyridyl-s-triazine. A micromethod was developed, which is generally well suited for automated, direct serum iron determinations, with respect to good flow properties, simple reagent composition, high reagent stability, rapid colour development, stable colour complex and high specificity. This method was run on either a Gilford System 203 S, Gilford Impact 400 or a Greiner G-400 analyser and adapted to the Technicon SMAC II, Technicon RA 1000, Eppendorf Epos and Abbott Spectrum automated systems. The tripyridyl-s-triazine method permits the determination of ferrioxamine iron in urine after a simple sample pretreatment.

Autoanalysis↗
PubMed1987

Determination of glycated hemoglobin by affinity chromatography.

An affinity chromatography microcolumn assay for glycated hemoglobin was compared with electrophoretic and microcolumn ion exchange methods. The affinity method has an imprecision of less than 4% for non-diabetic and less than 2% for diabetic specimens. The method is neither affected by carbamylated or acetylated hemoglobin nor by high glucose concentrations. Method comparisons showed discordant results due to interferences in electrophoretic and ion exchange methods in 3%-6.5% of all cases. Nonlinear relationships between affinity methods on one hand and electrophoretic as well as ion exchange methods on the other indicate that the affinity method measures not only beta-terminal glycated hemoglobin but all glycated hemoglobins, providing enhanced sensitivity and diagnostic value.

Blood Glucose↗
PubMed1984

Multiple forms of alkaline phosphatases in human liver tissue.

Alkaline phosphatases (AP) extracted in the presence of n-butanol from human liver are separated by affinity chromatography on phenylsepharose Cl-4B into two fractions named APII and APIIII. By repeated chromatography, APII was purified to a single enzyme entity with a specific activity of 1,684 kU/g protein. APIIII was purified to a specific activity of 535 kU/g protein. It consisted of only APIIII enzyme activity, but still contained gamma-glutamyltransferase activity. These two forms of AP are different in chromatographic and electrophoretic behaviour, APIIII being a larger molecule than APII. APII and APIIII are very similar in enzyme kinetic behavior, such as substrate activity, thermolability and sensitivity to different inhibitors. It is concluded from these experiments that multiple forms of AP in liver bear identical active centres, the difference is due to a modification of protein residue. It is possible that both are modified forms of one enzyme. Both are different from the AP isoenzyme that appears in serum in cholestatic patients.

Alkaline Phosphatase↗
PubMed1981

Alkaline phosphatase isoenzymes in serum of rats during cholestasis.

Alkaline phosphatase isoenzymes (API) in serum of rats during cholestasis are investigated. For comparison different membrane systems in liver are damaged. Proliferation of bile canaliculi, sinusoidal area, and endoplasmic reticulum, respectively, is induced by different toxic conditions. It is found that in cholestasis an API5 in serum arises which is not present in serum of normal rats, but can be detected in normal rat liver. Thus, it is not a de novo synthesis of this API. Under the condition connected with a proliferation of bile canaliculi we find this API5 in serum. Under different conditions without proliferation of bile canaliculi we do not find an increase of this API5. We assume, therefore, that API5 in cholestasis is produced by cells of the bile canaliculi rather than by liver parenchymal cells in the sinusoidal area. No difference is found in intra- or extrahepatic cholestasis.

Alkaline Phosphatase↗