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Biomedical subjects

C Mizon

Publications and source records attributed to C Mizon.

44 records · Page 3Linked to original sources
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↗
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↗
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↗