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Biomedical subjects

M Leclercq

Publications and source records attributed to M Leclercq.

At least 91 records · Page 5Linked to original sources
PubMed1979

Humoral antibody response to bovine leukemia virus infection in cattle and sheep.

In this study, 345 cattle from 7 herds with a history of lymphosarcoma were tested for antibody to BLV antigens by three serological methods, namely immunodiffusion using a bovine leukemia virus glycoprotein with a molecular weight of 60,000 as antigen, and radioimmunoassay using a bovine leukemia virus glycoprotein with a molecular weight of 60,000 and a bovine leukemia virus protein with a molecular weight of 24,000 as antigen. The three tests under comparison agreed for 335 animals, 240 being negative in the three tests, and 95 being positive. Results were variable in ten cases only. Glycoprotein with a molecular weight of 60,000 antibody titers were systematically higher than were protein with a molecular weight of 24,000 antibody titers in bovine sera and milk, as well as in sera of experimentally infected sheep. In the latter case, antibodies to bovine leukemia virus antigens reached maximal values at the animal death in the tumor phase of the disease. Ratios of serum antiglycoprotein titer to milk titer varied between 4 and 117, showing that, if milk pools are to be used in surveys of bovine leukemia virus infection, use of very sensitive techniques of detection is mandatory.

Animals↗
PubMed1977

The different electrophoretic forms of post gamma-globulin their antigenic identity and their structural variability.

Post gamma-globulin, first described as a constant component of protein of cerebrospinal fluid and urine from patients with tubular disorders has also been found in other biological fluids. Post gamma-globulin from a single individual always migrated as several bands after storage. Three electrophoretic forms, immunochemically identical, have been isolated by gel chromatography, preparative continuous flow electrophoresis and ion-exchange chromatography. Their molecular weight was found to be approximately between 11 000 to 12 000. No difference between the three forms could be detected. The N-terminal amino acids were found to be Lys, Arg and Leu respectively for the three forms of post gamma-globulin. The "slow" and "fast" forms of post gamma-globulin seemed to differ by elimination of small basic peptides or amino acids from the N-terminal end of the protein. No enzymatic activity of post gamma-globulin was found, but this requires further investigations.

Amino Acids↗
PubMed1975

Readenylation of polyadenylate-free globin messenger RNA restores its stability in vivo.

Using an ATP:RNA adenyltransferase from Escherichia coli, a polyadenylic sequence was resynthesized onto rabbit globin mRNA from which the poly (A) segment had been previously removed. Conditions for obtaining a homogenous reconstituted globin mRNA preparation containing 30 adenylic residues per message molecule were determined. The reconstituted globin mRNA was microinjected into Xenopus laevis oocytes. Its stability was very similar to that of native mRNA.

Adenine Nucleotides↗
PubMed1975

Absence of polyadenylate segment in globin messenger RNA accelerates its degradation in Xenopus oocytes.

Rabbit globin poly(A)-free and native mRNA preparations were microinjected into Xenopus oocytes. The amount of globin message remaining after incubation of injected oocytes was determined by molecular hybridization with a radioactive complementary DNA probe, synthesized by copying globin mRNA with purified RNA-dependent DNA polymerase (reverse transcriptase) from avian myeloblastosis virus. The results show that 56 hr after injection about 85% of the poly(A)-free mRNA molecules are degraded, while native poly(A)-containing mRNA chains are almost completely preserved during the same period of time.

Animals↗
PubMed1975

Low molecular weight proteinuria.

Low molecular weight (LMW) proteinurias vary widely in their microprotein composition. In general, there is little correlation between a given microprotein composition and a defined clinical disease (with the exception of the predominant beta-2-microglobulin in Wilson's disease). Free immunoglobulin light chains are a practically invariable component of, and may be the only detectable LMW protein in, 'tubular' proteinuria. The origins and significance of some frequently occurring urinary LMW proteins are discussed.

Adult↗