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Biomedical subjects

C Morel

Publications and source records attributed to C Morel.

At least 145 records · Page 8Linked to original sources
PubMed1975

Antibodies to herpes simplex virus types 1 and 2: a comparative study using indirect haemagglutination in carcinoma of the cervix and in other malignant conditions.

The authors used a technique of indirect haemagglutination to compare levels of antibody to Herpesvirus simplex types 1 and 2 in groups of patients with carcinoma of the cervix, together with other malignant conditions and in comparison to controls. A significant difference in the mean titre of antibody to type 2 virus is revealed between the carcinoma group and the B controls. The significance of the antibody assays is assessed by a study of the specificity of the antibodies found and by an assay of antibody which cross reacts with Herpesvirus simplex type 1.

Adult↗
PubMed1975

The secondary structure and poly(A) content of globin messenger RNA as a pure RNA and in polyribosome-derived ribonucleoprotein complexes.

The conformation in solution of duck and rabbit globin mRNA, and of the duck mRNA in the mRNA - protein particle, has been investigated by optical methods and also by the use of the dye ethidium bromide which becomes highly fluorescent when intercalated into the double-stranded regions of a nucleic acid. On the basis of the properties of this dye and on the ability of homopolyribonucleotides to form double-stranded structures we have, in addition, developed a simple and sensitive assay for the detection and quantitisation of sequences rich in a particular residue that may be present in an RNA chain. In solution, 45 to 60% of the nucleotides of duck globin nRNA were found to be in bihelical regions. A similar degree of secondary structure was found in rabbit globin mRNA (this paper), as well as in calf lens mRNA and mRNAs from ewe mammary gland (other results). All samples of globin mRNA examined in this work containeda sequence of poly(A), which has poly(U) binding properties similar to that of synthetic poly(a): no specific interaction between the poly(A) sequence and the rest of the molecules can be detected. The fraction of adenosine residues within these poly(A) segments represents 4% in rabbit mRNA and 8 to 9% in duck mRNA. An additional adenosine-rich segment interspersed with guanosine and possibly other residues, was also detected in one duck mRNA sample. The RNA in the duck mRNA - protein particle is also highly structured. The melting profile in the range of 20 to 65 degrees C is quite similar to that of free mRNA and the ability of ethidium bromide to intercalate is reduced to the extent of 70%. Yet the dichroic spectra of free and bound mRNA are significantly distinct. These data suggest that free and protein-bound mRNA May have a very similar degree of secondary structure but with distinct detailed conformation in bihelical regions (change in base tilting for example). Direct evidence has been obtained that proteins stick to the poly(A) segment in the particle since the fraction of adenosine residues detectable by our poly(u) titration procedure is reduced to 50% of that observed in the free mRNA.

Animals↗
PubMed1975

EDTA-and puromycin-derived duck- and rabbit globin-messenger ribonucleoprotein complexes isolated by oligo (dT)-cellulose chromatography.

Duck- and rabbit globin messenger ribonucleoprotein complexes isolated by oligo(dT) cellulose chromatography reveal an identical protein pattern-two main proteins of molecular weights of 73,000 and 49,000 daltons and minor components-whether the complexes have been liberated from polyribosomes with the EDTA- or the puromycin-high-salt method. In the globin messenger ribonucleoprotein particles of both species predominantly the protein with a molecular weight of 73,000 daltons is attached to poly(A)-containing regions of the messenger RNAs.

Animals↗
PubMed1975

Different sensitivities of avian- and mammalian-haemoglobin synthesis to elevated temperatures.

Avian- and mammalian-haemoglobin synthesis show different sensitivities to elevated temperatures. Temperature-dependent, reversible polyribosome disaggregation in avian cells occurs only at 45 degrees C, which is 3 degrees higher than the temperature for mammalian cells, and seems to be due to a block in the initiation of new polypeptide chains. The implications of these findings are discussed.

Animals↗
PubMed1974

Photoperiodism and enzyme activity: towards a model for the control of circadian metabolic rhythms in the crassulacean Acid metabolism.

Metabolic readjustments after a change from long days to short days appear, in Kalanchoe blossfeldiana, to be achieved through the operation of two main mechanisms: variation in enzyme capacity, and circadian rhythmicity. After a lag time, capacity in phosphoenolpyruvate carboxylase and capacity in aspartate aminotransferase increase exponentially and appear to be allometrically linked during 50 to 60 short days; then a sudden fall takes place in the activity of the former. Malic enzyme and alanine aminotransferase behave differently. Thus, the operation of the two sections of the pathway (before and after the malate step) give rise to a continuously changing functional compartmentation in the pathway. Circadian rhythmicity, on the other hand, produces time compartmentation through phase shifts and variation in amplitude, independently for each enzyme. These characteristics suggest that the operation of a so-called biological clock would be involved. We propose the hypothesis that feedback regulation would be more accurate and efficient when applied to an already oscillating, clock-controlled enzyme system.

Journal Article↗