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  • 1
    Electronic Resource
    Electronic Resource
    Alpha-1-Mikroglobulin in Urin und Serum bei Proteinurie und Niereninsuffizienz (1985)
    Springer
    Journal of molecular medicine 63 (1985), S. 711-717 
    Details
    ISSN: 1432-1440
    Keywords: Alpha-1-microglobulin ; Beta-2-microglobulin ; Proteinuria ; Renal insufficiency
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Alpha-1-microglobulin (alpha-1-m) is a low molecular weight glycoprotein (mw 25–33 KD) that is filtered through the glomeruli and reabsorbed in the proximal parts of the renal tubules where it is catabolized. Normal ranges were established for alpha-1-m (100 healthy controls) in serum (20–42 mg/l) and urine (3.5–8 mg/l). Alpha-1-m was then measured in 341 urine samples whose protein pattern had been classified as “pathologic” and “normal” according to microelectrophoresis. Increased alpha-1-m concentrations were found in 266 out of 280 pathologic urines (5% false negative) and in 3 out of 61 normal urines (4% false positive). Beta-2-microglobulin (beta-2-m), total protein or protein test strips showed a poorer correlation to the electrophoretic results. Measurement of alpha-1-m is, therefore, the most sensitive of these methods for the detection of proteinuria. In 90 patients with low molecular weight proteinuria and either with or without renal insufficiency alpha-1-m concentrations were determined in both urine and serum. While all patients had elevated urinary alpha-1-m concentrations, increased serum values were only found in renal insufficiency (Ccrea〈100 ml/min). Independently of these results, we were also able to establish that increased alpha-1-m levels are found at decreased glomerular filtration rates (Ccrea 〈70 ml/min). Pathologic alpha-1-m concentrations therefore only allow the conclusion of isolated tubular impairment when the GFR is greater than 70 ml/min. Data from 350 patients with various renal and hypertensive diseases showed that serum alpha-1-m is a more sensitive indicator of renal insufficiency, even in the so-called “creatinine blind” range (60–100 ml/min) of the GFR than either creatinine or beta-2-m.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01733115
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Plasma-Endothelin bei Normalpersonen und Patienten mit nephrologisch-rheumatologischen und kardiovaskulären Erkrankungen (1990)
    Springer
    Journal of molecular medicine 68 (1990), S. 774-779 
    Details
    ISSN: 1432-1440
    Keywords: Endothelin ; Hypertension ; Coronary artery disease ; Renal insufficiency ; Rheumatoid arthritis ; Lupus erythematodes ; Liver cirrhosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Plasma concentrations of the recently isolated potent vasoconstrictory peptide endothelin were measured in 382 patients. The investigations were performed by means of a sensitive radioimmunoassay specific for Endothelin-1, 2. The results from 110 healthy volunteers displayed a normal range of 44.67±3.51 pg/ml. Significantly raised levels were found in 33 patients with chronic end-stage renal failure both before and after hemodialysis. In contrast, 35 patients with compensated renal insufficiency did not differ from the normals. Sixty-five patients after kidney transplantation revealed significantly elevated levels, as did 27 patients with acute myocardial infarction, 8 after coronary bypass surgery, and 5 with liver cirrhosis. The mean values of 27 patients with untreated hypertension, 22 with secondary hypertension, of various causes and 16 with coronary artery disease were comparable to the normal population. The values were significantly decreased in 9 pregnant women with hypertension and proteinuria. A marked decline was found in 5 patients with systemic lupus erythematodes, while 20 patients with rheumatoid arthritis demonstrated only a slight decrease. The pathophysiological role of endothelin as a local or circulating hormone in regulating systemic blood pressure or release of other hormones remains to be determined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01647248
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Factors involved in the coordinate appearance of nitrite reductase and glutamine synthetase in the mustard (Sinapis alba L.) seedling (1990)
    Springer
    Planta 180 (1990), S. 429-434 
    Details
    ISSN: 1432-2048
    Keywords: Glutamine synthetase ; Nitrate (as inductor) ; Nitrite reductase ; Phytochrome (as inductor) ; Sinapis (nitrate assimilation)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The extent to which the appearances of nitrite reductase (NIR; EC 1.7.7.1) and glutamine synthetase (GS; EC 6.3.1.2) are coordinated was studied in mustard (Sinapis alba L.) seedlings. It was established by immunotitration that the increased activities of NIR and GS in the presence of light and nitrate can be attributed to the de-novo synthesis of enzyme protein. The bulk of the NIR and GS was found in the developing cotyledons. In the absence of nitrate in the growth medium there was no coordinate appearance of NIR and GS. While light strongly stimulated the appearance of GS, the level of NIR was hardly affected and remained low. On the other hand, in the presence of nitrate in the medium the appearances of NIR and GS were strictly coordinated, the GS level being considerably above that of NIR. It is argued that phytochrome-controlled synthesis of GS in the absence of nitrate is part of the mechanism to reassimilate ammonium liberated during proteolysis of storage protein and metabolism of the resulting amino acids, whereas the strictly coordinated synthesis in the presence of light and nitrate indicates the dominance of nitrate assimilation under these circumstances. The fact that the level of GS was always considerably above that of NIR appears to be a safety measure to prevent ammonium accumulation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01160400
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Factors involved in the coordinate appearance of nitrite reductase and glutamine synthetase in the mustard (Sinapis alba L.) seedling (1990)
    Springer
    Planta 180 (1990), S. 429-434 
    Details
    ISSN: 1432-2048
    Keywords: Glutamine synthetase ; Nitrate (as inductor) ; Nitrite reductase ; Phytochrome (as inductor) ; Sinapis (nitrate assimilation)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The extent to which the appearances of nitrite reductase (NIR; EC 1.7.7.1) and glutamine synthetase (GS; EC 6.3.1.2) are coordinated was studied in mustard (Sinapis alba L.) seedlings. It was established by immunotitration that the increased activities of NIR and GS in the presence of light and nitrate can be attributed to the de-novo synthesis of enzyme protein. The bulk of the NIR and GS was found in the developing cotyledons. In the absence of nitrate in the growth medium there was no coordinate appearance of NIR and GS. While light strongly stimulated the appearance of GS, the level of NIR was hardly affected and remained low. On the other hand, in the presence of nitrate in the medium the appearances of NIR and GS were strictly coordinated, the GS level being considerably above that of NIR. It is argued that phytochrome-controlled synthesis of GS in the absence of nitrate is part of the mechanism to reassimilate ammonium liberated during proteolysis of storage protein and metabolism of the resulting amino acids, whereas the strictly coordinated synthesis in the presence of light and nitrate indicates the dominance of nitrate assimilation under these circumstances. The fact that the level of GS was always considerably above that of NIR appears to be a safety measure to prevent ammonium accumulation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00198796
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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