Determination of aluminum in bone in haemodialyzed patients, using inductively coupled argon plasma emission spectrometry.

We propose a new method for measuring aluminium in bone tissue, using argon plasma emission spectrophotometry. The detection limit in the bone nitric digestion liquid was 0.015 mumol/l (corresponding to 0.

[Blood concentrations of maprotiline in depressive patients].

Blood levels of Maprotiline were analysed and their relationship to the clinical response was examined in 89 depressed inpatients, according DSM III criteria for Major Depressive Episode, given the drug treatment for 3 weeks. Maprotiline produced marked decreases in mean MADRS and COVI scale scores by the end of treatment. On day 21, no correlation between blood levels of Maprotiline and MADRS or COVI scores were found when all patients were considered.

Rapid determination of iron in urine, in the presence of deferoxamine, by inductively coupled plasma emission spectrometry.

Using a spectrometer with an argon plasma source coupled to a high-frequency magnetic field, we developed a direct method for determining iron in urine of patients being treated with deferoxamine. The detection limit for iron was 75 nmol/L; added iron was satisfactorily recovered; and we observed no interference from deferoxamine at its most commonly used concentrations. Values for between-run and within-run precision (CV) was less than 5%.

Swine liver L-leucine aminopeptidase: improved purification procedure.

An L-leucine aminopeptidase, having a specificity toward the substrate L-leucine amide, was purified 1084-fold from swine liver with a yield of 50.7 per cent. Purification procedure was carried out using successively centrifugation at 105 000 X g, fractionation by ammonium sulfate, DEAE Sephacel chromatography and zonal ultracentrifugation.

[Characterization of L-threonine deaminase activity of guinea pig liver induced by a high protein diet].

In a foregoing paper, we demonstrated that under equilibrated diet conditions, guinea pig liver L-threonine deaminase activity should be allocated to two distinct enzymes: a specific L-threonine deaminase without activity toward L-serine and a L-serine deaminase having a secondary activity toward L-threonine. In the present work, we observed that a high protidic diet caused an elevation of total threonine deaminase activity. Thus purification of guinea pig liver L-threonine deaminase was attempted, using ultracentrifugation, salt precipitation, heat treatment, ion exchange chromatography on DEAE Sephacel, Sephadex G 200 molecular sieve, 2 amino-2 methyl-1 propanol linked CH 4B Sepharose chromatography.

Human liver L-leucine aminopeptidase: evidence for two forms compared to pig liver enzyme.

Two forms of L-leucine aminopeptidase (E.C. 3.

Purification and enzymatic properties of an L-leucine aminopeptidase from swine liver.

An L-leucine aminopeptidase (alpha-aminoacyl-peptide hydrolase (cytosol), EC 3.4.11.

[Neutral leucinamidasic activity of human serum. Semiautomatic method of analysis].

Half automated method for determining a L-leucinamide splitting enzymatic activity in human sera. In normal and pathological human sera, two distinct L-leucinamide splitting enzymatic activities have been demonstrated. One of them has an optimal activity at pH 9 (alcaline leucine amidase activity) and shows the most properties of a classic leucinaminopeptidase (E.

[Guinea pig liver cytosol has an L-threonine deaminase activity distinct from L-serine deaminase].

Using sodium sulfate precipitation, "Sephadex G200" gel filtration and polyacrylamide gel electrophoresis, a L-threonine desaminase was demonstrated in the Guinea-Pig liver cytosol. This enzyme was separated from the guinea pig liver L-serine desaminase possessing an auxiliary activity on L-threonine substrate described by us in a previous work. The optimals for pH (7,1) and temperature (+ 55 degrees C) and the apparent molecular weight (134,000 + 20,000) were established.

Guine pig liver L-asparaginase. Separation, purification, and intracellular localisation of two distinct enzymatic activities.

Two distinct L-asparaginase (EC 3.5.1.

[Determination of blood iron and the total fixation capacity of transferrin by a simple automatic technic without dialysis].

An automated method without dialysis for determining serum iron is described. It is an adaptation of the Lauber procedure to the Technicon Auto Analyser I: serum iron is split from its protein combination by exposure to an acetate pH 5.8 buffer, in the presence of a detergent (Teepol 710) which prevents any precipitation of proteins.

[Semiautomatic method of measurement of serum 5'nucleotidase activity].

A semi-automated method for determining the 5'-nucleotidase activity in human serum for use with the Technicon Autoanalyzer I is described. Based upon the manual method of Persijn and Van Der Slik, adenosine formed by hydrolysis of 5'-AMP is deamined enzymatically and ammonia determined with the Berthelot reaction. The non specific alkaline phosphatases are inhibited by phenylphosphate.