| 1. |
- Back, S E, et al.
(författare)
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Age dependence of renal function: clearance of iohexol and p-amino hippurate in healthy males
- 1989
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Ingår i: Scandinavian Journal of Clinical & Laboratory Investigation. - 1502-7686. ; 49:7, s. 641-646
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Tidskriftsartikel (refereegranskat)abstract
- Iohexol, a newly developed non-ionic contrast agent, has been recently documented as a reliable glomerular filtration marker. This study describes the age dependence of the single injection clearance of iohexol in a sample of healthy male volunteers ranging from 21 to 77 years of age. In parallel, renal plasma flow was studied by measuring the total clearance of p-amino hippuric acid administered as a continuous infusion. In subjects older than 50 years a negative correlation to age was found for both p-amino hippuric acid and iohexol clearance, with a reduction of 52 ml/min and 12 ml/min per decade, respectively, whereas no age dependence was found for younger subjects. Correlation between p-amino hippuric acid and iohexol clearances was 0.81. However, the filtration fraction, defined as the ratio of iohexol to p-amino hippuric acid clearance, was higher in the elderly subjects. A consistent discrepancy was found between total and renal clearances of p-amino hippuric acid, indicating significant renal metabolism. Renal clearance of creatinine was poorly correlated to iohexol clearance and did not show any relationship to age.
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| 2. |
- Fagher, B, et al.
(författare)
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L-carnitine and haemodialysis: double blind study on muscle function and metabolism and peripheral nerve function
- 1985
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Ingår i: Scandinavian Journal of Clinical & Laboratory Investigation. - 1502-7686. ; 45:2, s. 169-178
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Tidskriftsartikel (refereegranskat)abstract
- Twenty-eight haemodialysis patients were randomized to L-carnitine, 2 g i.v. three times a week, and saline over a 6-week period. No obvious deficiency of carnitine was found in vastus lateralis with a median value of 12.9 mmol/kg dry weight; range 6.2-21.4. Female patients had lower total plasma carnitine compared to female controls, p less than 0.002, whereas no decrease was found in males. No relationship was found between muscle and total plasma carnitine. After carnitine administration the muscle carnitine level increased about 60%, p less than 0.01, and the total plasma carnitine level more than tenfold, whereas the initially high degree of acylation decreased, p less than 0.02. Maximum dynamic muscular strength was reduced with a mean value of 44% compared with healthy controls. Total metabolic activity of isolated skeletal muscle fibres, measured as heat production with a new technique using a perfusion microcalorimeter, showed a median value of 0.40 mW/g, 25% lower than normal, p less than 0.02. Carnitine administration had no effect on several different tests of muscular function. Neurophysiologically, discrete improvements in the temperature responses were recorded, but no changes in sensory and motor nerve conduction velocities or in vibration thresholds were noted. No symptomatic improvement was observed even in patients with the lowest carnitine levels prior to treatment. Our data do not support the hypothesis that carnitine deficiency contributes to muscle and nerve dysfunction in patients on chronic haemodialysis.
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| 3. |
- Herlitz, Johan, et al.
(författare)
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The diagnostic value of different enzymes and standard ECG in acute myocardial infarction
- 1985
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Ingår i: Scandinavian Journal of Clinical and Laboratory Investigation. - : Informa Healthcare. - 0036-5513 .- 1502-7686. ; 45:5, s. 413-420
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Tidskriftsartikel (refereegranskat)abstract
- Serum (S) enzyme activity of aspartate aminotransferase (ASAT, E.C. 2.6.1.1.), heat stable lactate dehydrogenase (LD, E.C. 1.1.1.27.), creatine kinase (CK, E.C. 2.7.3.2.) and CK-B subunit and the respective standard electrocardiograms (ECG) were compared in 463 patients with suspected acute myocardial infarction (MI) in order to evaluate sensitivity and specificity. Serum ASAT was analysed daily for 3 days, S-heat stable LD every 12 h for 48-108 h, S-CK and S-CK-B every 6 h for 48 h and ECG once daily for 3 days. All four enzymes had a high sensitivity, varying from 99% for LD to 97% for CK-B. The highest specificity was observed for CK-B and CK (98%) as compared with heat stable LD (91%) and ASAT (74%). Standard ECG showed a high specificity (96%) and a low sensitivity (80%).
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| 4. |
- Laurent, Torvald C., et al.
(författare)
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Urinary excretion of hyaluronan in man
- 1987
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Ingår i: Scandinavian Journal of Clinical and Laboratory Investigation. - 0036-5513 .- 1502-7686. ; 47:8, s. 793-799
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Tidskriftsartikel (refereegranskat)abstract
- A specific assay for hyaluronan (hyaluronic acid) has been applied to the determination of the polysaccharide in urine. The excretion in 22 healthy subjects was 330 micrograms/24 h (SD 77). The excretion was correlated with body weight and was therefore somewhat higher in males than in females. The molecular weight of the main fraction of urinary hyaluronan was in the range of 4000 to 12,000 in accordance with the hypothesis that it originates from blood and arises by glomerular filtration. A small fraction was of higher molecular weight and could have been produced in the urinary tract. Hyaluronan in male and female urine displayed the same molecular weight distributions. Patients with rheumatoid arthritis and primary biliary cirrhosis showed a two-fold and three-fold increase, respectively, of hyaluronan in urine with concurrently high levels of the polysaccharide in serum. A patient with Werner's syndrome displayed a ten-fold increase of the polysaccharide in both serum and urine.
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| 5. |
- Lilja, H., et al.
(författare)
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Characterization of the predominant basic protein in human seminal plasma, one cleavage product of the major seminal vesicle protein
- 1984
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Ingår i: Scandinavian Journal of Clinical and Laboratory Investigation. - : Informa UK Limited. - 0036-5513 .- 1502-7686. ; 44:5, s. 439-446
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Tidskriftsartikel (refereegranskat)abstract
- From liquefied human seminal plasma, we purified the predominant basic protein which appears following liquefaction of coagulated semen. The protein was purified in the presence of di-isopropylfluorophosphate to retard its degradation. Heparin-Sepharose® chromatography was followed by gel filtration (Biogel® P 60) and by fast performance liquid chromatography on a reversed phase column (C8). The basic protein is a single polypeptide chain with an apparent molecular mass of 12.8 kDa, and has a PI value between that of trypsinogen (9.3) and cytochrome C (10.3). The protein contains no carbohydrate, is rich in histidine, glutamate, and lysine, but is devoid of both cysteine and methionine. The amino-terminal portion of the protein sequence is unique: HNKQEGRDHDKSKG HFHRVVIHHKGGKAHRG-.A specific rabbit antiserum was raised against the 12.8 kDa basic protein. The protein was found to be unique to seminal plasma among all extracellular fluids examined. Three immunologically related 52 kDa, 71 kDa, and 76 kDa proteins were identified in seminal vesicle secretion when it had been reduced. Prostatic enzyme(s) degraded these proteins to the 12.8 kDa basic protein and several other basic proteins with apparent molecular masses below 18 kDa.
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| 6. |
- Lilja, H., et al.
(författare)
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Liquefaction of coagulated human semen
- 1984
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Ingår i: Scandinavian Journal of Clinical and Laboratory Investigation. - : Informa UK Limited. - 0036-5513 .- 1502-7686. ; 44:5, s. 447-452
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Tidskriftsartikel (refereegranskat)abstract
- Liquefaction of coagulated human semen was inhibited by o-phenanthroline; subsequent addition of Zn2+ reversed this inhibition, but not if the coagulum was repeatedly washed before Zn2+ was added. No liquefaction of the coagulum occurred when Fe2 was added (in a 1:3 molar ratio to o-phenanthroline), and the gel repeatedly washed. This o-phenanthroline-depleted coagulum was liquefied by resuspended pellet from ultracentrifuged pooled seminal plasma. In denatured and reduced semen coagulate, we identified the 52 kDa, 71 kDa, and 76 kDa protein bands of the predominant seminal vesicle protein. The protein was not present in the supernatant after centrifugation of coagulated semen, and it was degraded to several minor basic proteins when semen liquefied. These findings imply that the predominant seminal vesicle protein functions as the structural protein of coagulated semen. In much the same way as in ejaculated semen, the 52 kDa, 71 kDa, and 76 kDa protein bands in seminal vesicle secretion collected postmortem were digested to minor basic proteins after incubating the secretion with resuspended pellet from ultracentrifuged seminal plasma. This pellet contained the membrane-bound succinyl(alanine)3 -p- nitroanilide hydrolysing peptidase of prostatic origin which, like the liquefaction process, was active in the presence of EGTA, inhibited by non-chelated Zn2+, and inactivated by o-phenanthroline - an inactivation that was reversed by Zn2+.
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| 7. |
- Lilja, H.
(författare)
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Structure and function of prostatic- and seminal vesicle-secreted proteins involved in the gelation and liquefaction of human semen
- 1988
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Ingår i: Scandinavian Journal of Clinical and Laboratory Investigation. - : Informa UK Limited. - 0036-5513 .- 1502-7686. ; 48:S191, s. 13-20
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Tidskriftsartikel (refereegranskat)abstract
- At ejaculation, the epididymal spermatozoa mix with the secretions produced by the seminal vesicles and the prostate. The glandular secretions immediately turns into a gel-like structure which entraps the spermatozoa. The ejaculated spermatozoa become progressively motile as the gel dissolves. The discovery, structure, and interactions of proteins involved in these post-ejaculatory phase reactions of semen are here reported.
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| 8. |
- Lilja, H., et al.
(författare)
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Synthetic protease inhibitors and post-ejaculatory degradation of human semen proteins
- 1984
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Ingår i: Scandinavian Journal of Clinical and Laboratory Investigation. - : Informa UK Limited. - 0036-5513 .- 1502-7686. ; 44:5, s. 433-438
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Tidskriftsartikel (refereegranskat)abstract
- Normal post-ejaculatory proteolytic changes in human seminal plasma rapidly distort its electrophoretic protein pattern. This invalidates the electrophoretic evaluation of the content in the secretion from the accessory sex glands. Both agarose and sodium dodecylsulphate polyacrylamide gel electrophoresis (SDS-PAGE) were used to study the proteolytic changes and how they could be modified by various synthetic protease inhibitors. Liquefaction of coagulated semen could be inhibited by adding o-phenanthroline directly after ejaculation, whereas neither neutrally buffered Na2EDTA, di-isopropylfluorophosphate (DFP), benzamidine, nor thiol reagents proved effective. Addition of the serine protease inhibitors DFP and benzamidine, o-phenanthroline, and iodoacetamide substantially retarded the proteolytic alterations of the proteins as demonstrated by both agarose electrophoresis and SDS-PAGE. We recommend that electrophoretic protein analysis of human semen be performed on ejaculates collected in vessels containing protease inhibitors. For routine analysis, the addition of benzamidine ensures sufficiently stable proteins to permit reliable electrophoretic analysis of samples stored at room temperature for 4 h.
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| 9. |
- Lilja, H., et al.
(författare)
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The predominant protein in human seminal coagulate
- 1985
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Ingår i: Scandinavian Journal of Clinical and Laboratory Investigation. - : Informa UK Limited. - 0036-5513 .- 1502-7686. ; 45:7, s. 635-641
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Tidskriftsartikel (refereegranskat)abstract
- The predominant protein in human seminal vesicle secretion constitutes the structural protein of coagulated semen. This high molecular weight protein (HMW-SV-protein) is stable in seminal vesicle secretion during in vitro storage at 37 d̀C for at least 20 h, but is rapidly cleaved on mixing with prostatic proteases. Seminal coagulate, washed free of souble components, is dissoluble by 2 to 3 mol/1 of guanidine-HCl. Although dithiothreitol added to seminal coagulate does not liquify the clot, complexes between HMW-SV-proteins are broken up by reduction under denaturing conditions, which suggests that the non-covalent linkages of HMW-SV-proteins are essential in the clot. Prostatic proteases cleave the HMW-SV-protein during liquefaction of ejaculated semen to a series of labile proteins. These proteins are further cleaved to peptides of successively decreasing size after completed liquefaction. The cleavage of the HMW-SV-protein is the major cause of the fast shift of the electrophoretic pattern of seminal proteins if semen is stored without protease inhibitors.
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| 10. |
- Lindqvist, Ulla, et al.
(författare)
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The diurnal variation of serum hyaluronan in health and disease
- 1988
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Ingår i: Scandinavian Journal of Clinical and Laboratory Investigation. - 0036-5513 .- 1502-7686. ; 48:8, s. 765-770
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Tidskriftsartikel (refereegranskat)abstract
- The variation of the serum concentration of hyaluronan during the day and between days has been investigated. In a group of healthy volunteers, the mean hyaluronan level was very stable over time except for a moderate but significant elevation after rising from bed in the morning. Patients with rheumatoid arthritis showed markedly increased hyaluronan concentrations 0.5-2 h after leaving bed. Patients with primary biliary cirrhosis exhibited high and rather constant levels during the day. A reference group of hospitalized patients with other diseases did not show any diurnal variation. The best reproducibility in hyaluronan determinations is obtained if specimens are taken before the subjects rise from bed or a few hours later, i.e. after the morning elevation of serum hyaluronan has subsided. In rheumatoid arthritis valuable information can be obtained by repeated sampling during the morning hours.
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