PubMed HealthSearch

Biomedical subjects

B M de Bornier

Publications and source records attributed to B M de Bornier.

4 recordsLinked to original sources

Experimental studies on unconjugated bilirubin binding by human erythrocytes.

The evaluation of the bilirubin bound to human erythrocytes is considered by some paediatricians as a test to estimate the risk of development of kernicterus. We have studied the physical and chemical characteristics of this binding. Red blood cell membranes contain specific binding sites for bilirubin, the affinity of which is low (Kd = 170 mumol/L). The dissociation constant of the bilirubin/human serum albumin complex is about 10,000 times lower. In jaundiced neonates even with a level of blood bilirubin higher than 300 mumol/l, the binding of bilirubin to red blood cells is negligible. So, the evaluation of the bilirubin bound to human red blood cells does not seem to be a useful test to appreciate the risk of development of kernicterus.

Adult

Uroporphyrinogen I synthase assay as an evaluation of the in vitro development of human BFU-E and CFU-E.

We describe a simple spectrophotometric microassay to quantify the proliferation and the differentiation of human bone marrow or blood erythroid progenitor cells CFU-E and BFU-E. These precursors give rise, in culture, to colonies and bursts with markedly variations in size and hemoglobinization, which cannot be accurately evaluated by the usual method of scoring. We then developed a sensitive biochemical microassay to measure the uroporphyrinogen I synthase activity of progenitors grown in small wells. This assay is a valuable index of erythroid differentiation in vitro. This method can offer the opportunity to test the efficiency in vitro of various therapeutic agents in patients with hemopoietic disorders.

Ammonia-Lyases

2,3-2, 3-.

Erythrocityc variations of glycolytic intermediates and 2,3-DPG levels in rabbits performing strenuous exercise under hypoxic conditions are correlated with blood pH variations. The hypoxia alone is not able to induce directly an increase of erythrocytic 2,3-DPG level which would facilitate tissue oxygenation.

Animals