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Biomedical subjects

D Combes

Publications and source records attributed to D Combes.

40 records · Page 3Linked to original sources

Platelets in myeloproliferative disorders. I. A comparative evaluation with certain platelet function tests.

Certain platelet functions were evaluated in 24 patients with secondary polycythaemia (SP) and in a large number of patients suffering from myeloproliferative disorders (MD'S): 89 patients with chronic myeloid leukaemia (CML) at different stages of development, 58 with polycythaemia vera (PV), 23 with essential thrombocythaemia (ET), and 25 with agnogenic myeloid metaplasia (AMM). Bleeding time, epinephrine-induced platelet aggregation and adhesiveness agreed with those generally reported in the literature; they are independent of thrombocytosis, the haemoglobin level and the leucocyte count. Macrothrombocytosis, evaluated by an electronic method, was only found in CML, mainly during acute blast crisis. An increased percentage of light platelets was a constant feature in all groups except in the SP and in 20% of the PV. The most severe abnormalities were observed in AMM and CML in the acute stage; in the chronic phase of CML there is no correlation between the severity of platelet abnormalities and the survival of the patients.

Blood Platelets↗

Effect of different proteases on bitterness of hemoglobin hydrolysates.

Hemoglobin was hydrolyzed by several enzymes (Proctase, Alcalase, Neutrase, papain). Hydrolysates were analyzed (degree of hydrolysis, gel permeation on Superose 12 column, tasting) and fractionated by ultrafiltration and 2-butanol extraction. The bitter peptides were isolated and identified. The results were compared with those already obtained with peptic hemoglobin hydrolysates. All the findings were confirmed. Ultrafiltration concentrated bitter compounds in the fraction corresponding to 500-5000 Da, and these compounds were selectively extracted by 2-butanol. All the bitter peptides belonged to the same fragment of the beta-chain of bovine hemoglobin. Finally, the use of a Superose 12 chromatographic column for easy detection of bitter hydrolysates without sensory analysis could be generalized for hemoglobin hydrolysates.

Amino Acid Sequence↗

Four acetylcholinesterase genes in the nematode Caenorhabditis elegans.

Whereas a single gene encodes acetylcholinesterase (AChE) in vertebrates and most insect species, four distinct genes have been cloned and characterized in the nematode Caenorhabditis elegans. We found that ace-1 (mapped to chromosome X) is prominently expressed in muscle cells whereas ace-2 (located on chromosome I) is mainly expressed in neurons. Ace-x and ace-y genes are located in close proximity on chromosome II where they are separated by only a few hundred base pairs. The role of these two genes is still unknown.

Acetylcholinesterase↗