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B A Morgan

Publications and source records attributed to B A Morgan.

71 records · Page 4Linked to original sources

Delimiting regulatory sequences of the Drosophila melanogaster Ddc gene.

We delimited sequences necessary for in vivo expression of the Drosophila melanogaster dopa decarboxylase gene Ddc. The expression of in vitro-altered genes was assayed following germ line integration via P-element vectors. Sequences between -209 and -24 were necessary for normally regulated expression, although genes lacking these sequences could be expressed at 10 to 50% of wild-type levels at specific developmental times. These genes showed components of normal developmental expression, which suggests that they retain some regulatory elements. All Ddc genes lacking the normal immediate 5'-flanking sequences were grossly deficient in larval central nervous system expression. Thus, this upstream region must contain at least one element necessary for this expression. A mutated Ddc gene without a normal TATA boxlike sequence used the normal RNA start points, indicating that this sequences is not required for start point specificity.

Alcohol Dehydrogenase↗

The wild-type nucleotide sequence of the rpoBC-attenuator region of Escherichia coli DNA and its implications for the nature of the rifd18 mutation.

To investigate the possibility that the unusual dominant rifampicin-resistance characteristic of the rifd18 allele of E. coli rpoB is due to a secondary, regulatory mutation, we have determined the nucleotide sequence of a 1.1 Kbp wild-type DNA fragment, including the transcriptional attenuator and translational start-site of rpoB. We have also re-investigated the previously published sequences of this region in lambda rifd18 and lambda rifd47 DNA. Our results indicate that all three sequences are identical, and reveal some errors in the published data. We discuss the basis of dominance of rifd18.

Alleles↗

The cloned dopa decarboxylase gene is developmentally regulated when reintegrated into the Drosophila genome.

The Drosophila dopa decarboxylase gene, Ddc, functions normally when reintroduced into flies. DNA containing a cloned Ddc gene inserted into a P element transposon was injected into early embryos. Transformants were identified by suppression of the cuticular phenotype of a Ddc mutant allele. The reintegrated genes are expressed in the proper tissue and at the proper stages during development even though their positions within the genome are different from that of the wild-type Ddc gene. Absolute levels of DDC enzyme activity are within 35% of that found in wild-type Canton S flies, the source of the transforming DNA. The transformants' Ddc RNA is indistinguishable from that of wild type. One reintegrated Ddc gene, inserted on the X chromosome, is affected by the dosage compensation mechanism that leads to sex-specific differences in the expression of many X-chromosome genes.

Animals↗

Analogues of beta-LPH61-64 possessing selective agonist activity at mu-opiate receptors.

Peptides based in the stabilised tetrapeptide HTyr-D-Ala-Gly-MePheOH have been synthesised and shown to have substantial opioid activity both in vitro and in vivo. The selectivity of these compounds of different receptor populations has been investigated using both isolated tissue assays and binding studies. Results suggest that the compounds are potent agonists at mu-receptors with little or no affinity for the delta-receptor population. One of the compounds, RX783006 (HTyr-D-Ala-Gly-MePhe-NH(CH2)2OH), has been tritiated to high specific radioactivity and may prove to be a useful probe in the elucidation of the function of the heterogenous opiate receptor population.

Animals↗

Effect of synthetic thyrotrophin-releasing hormone and its analogues on growth hormone secretion in the domestic fowl (Gallus domesticus).

Variations in plasma growth hormone (GH) concentrations following iv or sc administration of synthetic thyrotrophin-releasing hormone (TRH, Pyr-His-Pro-NH2) have been followed in immature and adult domestic fowl. TRH markedly stimulated GH secretion in newly hatched (1 and 2 day old) chicks and in 6-week-old cockerels but in adult male or female birds of two strains had very little effect, if any. Intravenous injection of 4 TRH analogues (Pyr-His-Mep-NH2, Pyr-Meh-Mep-NH2, Pyr-Meh-Mep-NH and Pyr-Meh-Pro-NH2) were also potent GH secretagogues in 6-week-old birds. The stimulatory effect of TRH or the TRH-analogues on GH secretion was not dose-related.

Age Factors↗

Modification of the proline residue of TRH enhances biological activity and inhibits degradation.

An analogue of TRH with a modified proline residue (Pyr-His-MepNH2) has been synthesised and evaluated. In CNS, but not endocrine tests the analogue had improved activity compared to TRH and was more resistant to enzymatic degradation. A metabolite of TRH, His-Pro, was without biological activity. It is concluded that the biological actions attributed to TRH are due to the parent tripeptide rather than His-Pro and that these actions can be enhanced by improving the biological stability of TRH.

Animals↗