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Biomedical subjects

J Mizon

Publications and source records attributed to J Mizon.

At least 55 records · Page 3Linked to original sources
PubMed1989

[Antitrypsin activity of the urine and alpha 1 protease inhibitor].

The urinary trypsin inhibitory capacity (TIC) is mainly due to the excretion of an inhibitor which is immunologically related to inter-alpha:trypsin inhibitor (ITI). However, alpha 1 protease inhibitor (alpha 1 PI) can be found in urine of patients with proteinuria. When this one is greater than 1 g/l, the measured TIC is more or less markedly related to the amount of alpha 1 PI present in the analyzed sample. The antitryptic activity of alpha 1 PI can be ruled out by incubating urine with specific anti-alpha 1 PI immunoglobulins. An identical result is obtained by acidification of the sample prior to TIC determination. Moreover, after freezing of urine, only the antitryptic activity of alpha 1 PI is strikingly decreased. Thus, in the presence of a significant proteinuria (greater than 1 g/l), a preliminary acidification of urine allows a suitable and specific measurement of TIC due to the inhibitor immunologically related to ITI. Thus, this one is a sensitive, useful and easy test for detecting and monitoring infections.

Bacterial Infections↗
PubMed1988

Plasma proteins immunologically related to inter-alpha-trypsin inhibitor.

SDS-polyacrylamide gel electrophoresis and immunoblot were applied to analysis of plasma proteins immunologically related to inter-alpha-trypsin inhibitor (ITI). In this system, anti-ITI sera were able to identify ITI and other components with an Mr near 120 kDa which would be degradation products of ITI by limited proteolysis. An anti-UTI (urinary trypsin-inhibitor) serum could detect, beside these derivatives, two minor components (Mr values near 90 and 60 kDa). Analysis of perchloric acid supernatants of plasma samples, using the same technic, induced visualization of a new component, similar to urinary trypsin inhibitor which could not be detected by direct analysis. This one was also characterized in a higher content in pathological samples (renal failure and infectious diseases).

Alpha-Globulins↗
PubMed1988

[Clinical value of the determination of urinary antitrypsin activity].

Urinary trypsin inhibitory capacity is mainly due to the excretion of a glycoprotein which is immunologically related to the inter alpha-trypsin inhibitor and may be a proteolytic degradation product of that substance. It was tested in 133 subjects divided into 7 groups: 24 healthy controls (group A), 21 patients with bacterial infection (group B), 37 with bacterial infection under antibiotic therapy (group C), 25 with connective tissue disease (group D), 8 with infected connective tissue disease (group E), 14 with cancer (group F) and 4 with infected cancer (group G). Urinary trypsin inhibitory capacity level was very low in controls (3.32 +/- 0.8 U/g urinary creatinine), but it was dramatically increased when infection was present (149.67 +/- 23.6 U/g urinary creatinine). This test appeared to be more effective than serum C-protein measurement simultaneous carried out in the same patients. Urinary trypsin inhibitory capacity is not related to the degree of proteinuria in the urine sample, but it is increased in patients with chronic renal failure excluded from this study. Thus, its measurement is a sensitive, easy and useful test for detecting and monitoring infections. The return to its physiological value is a very good argument in favour of therapeutic effectiveness.

Bacterial Infections↗
PubMed1988

Qualitative study of fecal alpha 1-proteinase inhibitor in normal subjects and patients with Crohn's disease.

We applied sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and immunoblotting to analyze fecal alpha 1-proteinase inhibitor (alpha 1 PI) from healthy subjects and patients with Crohn's disease. A component with Mr 38,000 was characterized in normal fecal extracts as well as in six pathological samples. In these cases, the Crohn's disease activity index (CDAI), a clinical index of severity of the disease, was 170 (SEM 47). In contrast, alpha 1 PI of Mr 51,000 was detected in fecal extracts from eight patients with active Crohn's disease (CDAI = 287, SEM 39). We conclude that fecal alpha 1 PI can be considered a marker of intestinal disease activity.

Adolescent↗
PubMed1987

The effect of the glycosaminoglycan chain removal on some properties of the human urinary trypsin inhibitor.

The major urinary trypsin inhibitor UTI I is a proteoglycan. UTI c (Mr 26,000), produced by chrondroitin lyase digestion of UTI I, was isolated and characterized. About 90% of the glycosaminoglycan chain was removed by this treatment without proteolytic modification, as assessed by amino-acid composition and N-terminal sequence of UTI c. Its electrophoretic mobilities on alkaline and SDS-PAGE are identical with those of UTI II which occurs in urine during storage. To study the role of the glycosaminoglycan chain on the inhibitory properties of UTI I, UTI I and UTI c were compared using different proteinases as target enzymes. The inhibitory activity towards bovine trypsin and chymotrypsin as well as human granulocytic cathepsin G did not differ significantly. However, towards human granulocytic elastase, the equilibrium dissociation constant (Ki) is 5 times higher for UTI c than for UTI I. Weak inhibitory activities were measured on human plasmin, UTI c being more efficient than UTI I. The acid-stability of UTI I is not modified after chrondroitin lyase treatment. UTI I and UTI c are equally sensitive to trypsinolysis indicating that the covalently bound glycosaminoglycan chain does not play an important role for the stability of UTI I.

Cathepsin G↗
PubMed1986

The major human urinary trypsin inhibitor is a proteoglycan.

The major urinary trypsin inhibitor (Mr 44 000), isolated from human urine, contains 35% carbohydrate. In addition to N-acetylglucosamine and neutral sugars (primarily mannose and galactose), the carbohydrate moiety contains hexuronic acid and N-acetylgalactosamine and corresponds to a glycosaminoglycan. This carbohydrate chain is an integral component of the inhibitor: it does not dissociate from the inhibitor when using dissociative conditions such as sodium dodecyl sulfate, guanidinium chloride, or by increasing ionic strength or mixing with cetylpyridinium chloride. This glycosaminoglycan chain is sensitive to chondroitinase ABC or testicular hyaluronidase digestion and corresponds to slightly sulfated chondroitin 4-sulfate or 6-sulfate. After treatment by these enzymes, the urinary inhibitor has a lower molecular mass (Mr 26 000) but still inhibits trypsin.

Amino Acids↗
PubMed1985

Human urinary proteinase inhibitor: inhibitory properties and interaction with bovine trypsin.

The major urinary trypsin inhibitor (UTI) was found to inhibit bovine chymotrypsin and human leucocyte elastase strongly, cathepsin G weakly. No inhibition of porcine pancreatic elastase was observed. The stoichiometry of the inhibition of bovine trypsin by UTI was determined spectrophotometrically to be 1:2 (I/E molar ratio). After incubation of UTI with this enzyme in various molar ratios, two complexes (C1 and C2) could be visualized in alkaline polyacrylamide gel electrophoresis. C1 was isolated by affinity chromatography on Con-A Sepharose. In dodecyl sulfate polyacrylamide gel electrophoresis, C1 was dissociated to give an inhibitory band with the same electrophoretic mobility as native UTI. C2 released an active inhibitory fragment with Mr near 20000. A time-course study demonstrated that at a molar ratio I/E of 1.5:1, the C2 complex appears after two hours of incubation.

Animals↗
PubMed1983

Urinary trypsin inhibitory capacity determination: study in patients with disseminated cancers.

We present a method for automated analysis of urinary trypsin inhibitory capacity. The validity of the method has been established. The mean value of urinary antitryptic activity is higher in patients with disseminated cancers (70 IU/1, n = 243) than in healthy donors (14,4 IU/1, n = 117). However, frequency distribution of urinary trypsin inhibitor values shows a great overlap, so that an increased level of urinary trypsin inhibitor cannot be considered as a marker of neoplastic diseases but seems to be a non specific indicator of inflammatory syndromes.

Adult↗
PubMed1981

[Continuous-flow determination of delta-aminolevulinic acid in urine (author's transl)].

The automatic determination of urinary ALA using a continuous flow methodology, is described. The amplification of the measured signal, with an adjusted range expander, allows to reduce the sample volume and to decrease drastically the effects of interfering substances. The results are compared with the reference method of Davis and Andelman [11].

Aminolevulinic Acid↗
PubMed1980

Rapid sodium dodecyl sulfat/polyacrylamide gel electrophoresis of urinary proteins.

We describe a procedure for the convenient separation of proteins by sodium dodecyl sulfate/polyacrylamide gel electrophoresis of urine from cases of renal disease. A precipitation method that requires no special apparatus was used to concentrate the urinary proteins; for electrophoretic separation we used a commercially supplied polyacrylamide/cellulose gel slab. This method seems to be valuable for investigation of proteinuria; we recommend it for routine use.

Chemical Precipitation↗
PubMed1979

[Purification and characterization of protease inhibitors from urine during pregnancy (author's transl)].

Two forms of urinary trypsin inhibitor, A and B, were purified from the pooled urine from pregnant women using non-denaturing methods. The inhibitor B arose from the inhibitor A and was not present in native urine. Electrophoresis on polyacrylamide gel in the presence of sodium dodecyl sulfate indicated a new heterogeneity of the inhibitor B with molecular weights of 33 000 and 24 000; the molecular weight obtained for the inhibitor A was 50 000. Inhibitors A and B were acidic proteins with an isoelectric pH of about 2.6 for A and about 4.2 for B. Inhibitor A and inter-alpha-trypsin inhibitor formed a precipitate with an antiserum to purified inhibitor B. But neither inhibitor A nor inhibitor B formed a precipitate with anti whole human serum or anti-inter-alpha-trypsin inhibitor antiserum. Measurements of specific activity of inhibitor A were consistent with two active sites in the molecule.

Chromatography↗
PubMed1979

[Application of adsorption chromatography to the colorimetric determination of urinary estrogens in late pregnancy (author's transl)].

A new extraction procedure of urinary estrogens, based upon adsorption chromatography on Amberlite XAD-2, was deviced for a selective and complete extraction of these components. Estrogens were then quantified, without preliminar hydrolysis, by the colorimetric Kober reaction, modified by Ittrich. The reliability of this method has been established by comparison with four other methods.

Adsorption↗
PubMed1978

[Application of polyacrylamide gel electrophoresis-SDS to the study of proteinuria (author's transl)].

The authors present a variant of the technique of sodium dodecylsulfate acrylamide gel electrophoresis (SDS-PAA) reported by Weber and Osborn, for the analysis of urinary proteins. SDS-PAA separates the proteins chiefly according to their molecular radius. SDS-PAA, as compared to acetate cellulose electrophoresis and immunoelectrophoresis, gives better resolution and may be recommended for the investigation of proteinuria.

Electrophoresis, Cellulose Acetate↗