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J M Delabar

Publications and source records attributed to J M Delabar.

41 records · Page 3Linked to original sources
PubMed1986

Rearrangement of chromosome 21 in Alzheimer's disease.

We have analyzed the DNA from four patients suffering from a dementia of the Alzheimer type and of four controls of identical age. Estimates of the copy numbers of two genes located on chromosome 21, SOD1 and ETS2, gave the following results: in all the cases there was duplication of ETS2 whereas SOD1 was normal. These preliminary results indicate that the segment of chromosome 21(q21----q22.1) is rearranged in all the four patients who were investigated.

Alzheimer Disease↗
PubMed1985

Nonrandom location of H1-H1 degree histones on chromatin of mouse liver and brain.

The electrophoretic behavior of nucleosome dimers reconstituted with H1 or H1 degrees and the features of the digestion of those reconstituted dimers with micrococcal nuclease were first investigated. Both criteria appear to support the notion that H1 degrees can replace H1 on the nucleosome on a one-to-one basis and that both proteins fulfill a similar structural role in chromatin. H1/H1 degrees ratios in different chromatin subfractions from mouse liver were then indirectly measured by means of an electrophoretic purification of H1 degrees- from H1-containing nucleosome monomers, followed by a titration of different specific nucleotide sequences in the corresponding DNAs. Satellite and globin containing chromatin subfractions were found to contain only about half the amount of H1 degrees which is normally encountered in bulk chromatin, indicating a nonrandom location of H1-H1 degrees variants on untranscribed sequences; in contrast, titrations with cDNA from poly(A+) RNA and albumin cDNA show an approximately 2-fold enrichment in H1 degrees for the corresponding chromatin when compared to the same bulk chromatin. In the brain, inactive albumin chromatin contains a relative amount of both H1 variants similar to that found in satellite or globin chromatin in liver. Amounts of H1 degrees can, therefore, be correlated with different states of chromatin: an inactive state with a lower amount of H1 degrees and a potentially active state with an enrichment in H1 degrees.

Albumins↗
PubMed1982

The binding of NADH and NADPH to bovine-liver glutamate dehydrogenase. Spectroscopic characterisation.

1. The binding of NADH and NADPH to bovine liver glutamate dehydrogenase has been studied using circular dichroism (CD) and fluorescence spectroscopy, under comparable conditions of enzyme concentration. Spectroscopic titrations have been analysed using non-linear least-squares techniques to determine dissociation constants and parameters for the different chromophoric portions of the bound coenzymes, according to different models for the binding equilibria. 2. For NADPH, enhancement of dihydronicotinamide fluorescence and positive CD at 340 nm reflect binding of the coenzyme at the active site (site I) via the dihydronicotinamide moiety with a dissociation constant K1 of 50 microM; negative CD at 260 nm reflects the binding of a second molecule of coenzyme at the non-active site (site II) via the adenine moiety with a KII of 650 microM. 3. For NADH, the same spectroscopic assignment is made; however, site II affinity is much greater (KII 20 microM) and exceeds the affinity at the active site (KI 50 microM). 4. In no case was spectroscopic evidence obtained with either coenzyme to support the concept of non-identical active site binding as three sites IA and three sites IB per hexamer. 5. Coenzyme affinities are approximately twofold higher in triethanolamine buffer (0.05 + 0.1 M KCl, pH 7.6) compared with phosphate buffer (0.1 M at pH 7.0). 6. ADP enhances the CD of bound NADPH at 340 nm by up to twofold; phosphate ion also enhances the CD and binds with a Kd of 60-80 mM. GTP causes strong negative CD at 340 nm but only for the NADPH bound at site II. These results are consistent with independent binding sites for ADP (site II) and GTP (site III); phosphate ion is apparently able to affect certain properties of all three sites.

Animals↗