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Biomedical subjects

M Blanc

Publications and source records attributed to M Blanc.

At least 127 records · Page 7Linked to original sources
PubMed1981

[Value of the determination of urinary 3-methylhistidine (3 MEHIS) in the evaluation of postoperative muscular catabolism].

Daily estimations of urinary 3 methylhistidine, creatinine and total nitrogen were carried out during the first four post-operative days in sixteen patients who had undergone uncomplicated abdominal surgery and receiving parenteral alimentation. Figures obtained for 3 methylhistidine (19.36 +/- 4.48 mumol/kg as a cumulative for the 4 days) could be used to assess the catabolism of muscular protein during this period at approximately 320 g for a 70 kg subject, i.e. approximately twice that found in the healthy adult. There was a good correlation between 3 MEHIS and creatinine. Muscular catabolism is hence proportional to the degree of lean body mass. By contrast, there was no correlation between the excretion of 3 MEHIS and nitrogen excretion. Finally, study of the effect of qualitative and quantitative variations in nitrogen intake on muscular proteolysis did not make possible any conclusion at present. Further studies are hence necessary.

Abdomen↗
PubMed1980

Fatty acids bound to serumalbumin decrease the half-life of thromboxane A2.

The half-life of thromboxane A2 is increased in plasma as well as in a buffer containing serumalbumin. Moreover, the half-life of thromboxane A2 depends on the amount of unesterified fatty acids bound to albumin. When more fatty acids are bound, the half-life is shortened. This shortening is accompanied by a decrease of the aggregating activity of thromboxane A2.

Chemical Phenomena↗
PubMed1980

[Branched amino acids. Role and value in parenteral nutrition].

The authors undertook a general review of the principal studies concerning branched amino acid (B.A.A.) and justifying their use in large doses during parenteral alimentation. Certain particular features emerge concerning valine, isoleucine and leucine which render these three amino acids particularly valuable:--their metabolism is essentially mascular and they escape hepatic control in great part, in contrast to other amion acids;--broken down by muscle, they represent a significant source of energy, sometimes the only available, but may also be used in numerous metabolic processes;--particularly sensitive to hormonal actions, their metabolism is in addition regulated by different non-hormonal factors;--their regulatory role of insulin secretion is considered to be important by many authors;--their original behaviour in certain pathological circumstances, and in particular in malnutrition states, the post-agressive phase and in hepatic failure, has resulted in progress in the physiopathology of these pathological states and above all led to valuable therapeutic deductions;--their toxicity is negligeable and they may be given in large amounts during parenteral alimentation without causin intolerance reactions or severe disturbances in plasma aminograms.

Amino Acids, Branched-Chain↗
PubMed1980

Antiglobulins in normal human sera which react with baboon Ig G.

Antiglobulins of the Ig M class which react with the Ig G of baboons have been discovered in approximately half the number of normal human sera investigated by the technique of hemagglutination of red blood cells coated with baboon immune serum. The frequency of these antiglobulins is significantly higher among patients suffering from seropositive rheumatoid arthritis but there is no correlation with the presence of Milgröm-type antiglobulins. The inhibition of several sera containing these antiglobulins by the sera of baboon of different species is also reported.

Animals↗
PubMed1978

Lymphocytotoxic antibodies and antiglobulins in renal allograft recipients. Correlative study with acute rejection.

In 45 patients who received kidney transplants, both homologous and heterologous human antiglobulins (anti-Ig) and HLA cytotoxic antibodies have been studied before and after transplantation and in some cases after nephrectomy. A similar study has been performed in a control group of 1,019 healthy blood donors and in 130 patients with acute or chronic glomerulonephritis. After transplantation, homologous anti-IgG were found in 60% of the patients, as compared with 3.5% in the healthy blood donors and 21% in patients with various forms of glomerulonephritis. This difference is particularly striking in sera obtained prior to nephrectomy; the presence of anti-IgG and cytotoxic antibodies in the same patient being significantly associated with early transplant failure. Anti-IgA were found in 75% of the patients with transplants and in 37% of the patients with glomerulonephritis. There was no relationship between the anti-IgA and the outcome of the graft. On the other hand, heterologous anti-Ig were unchanged in the three groups investigated. The mechanism of formation of the anti-IgG is not clear. They are probably antibodies against antigenic structures of the patient's own antibodies, previously combined with a soluble antigen or an antigen on the transplant that has undergone molecular transformation in the course of this reaction. Their pathogenic role, although not demonstrated, can be strongly suspected, and, in a practical way, screening for the anti-Ig in kidney transplant recipients could be of value as a prognostic test.

Antibodies↗
PubMed1977

Human IgG3 allotypes, with special reference to a new allotype related to G3m(g) (G3m21).

The IgG3 allotype described as L1 (Blanc et al., 1976) occurs on the CH3 region of G3m(g) proteins, in contrast to G3m(g) that is known to be present on the CH2 region. G3m(g) and L1 are, as a rule, present on the same gamma3 heavy chain, just like the G3m(b) subspecificities of the CH2 region, (b1) and (b4), with those of the CH3 region (b0), (b3) and (b5). Several families were investigated that showed inheritance of rare combinations of IgG3 allotypes. The data obtained are suggestive for notation of L1 as (g5), since L1 probably occupies a position antithetical to (b5). The relation of amino acid substitutions to allotypes and isoallotypes is discussed.

Alleles↗