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D T Sullivan

Publications and source records attributed to D T Sullivan.

51 records · Page 3Linked to original sources
PubMed1976

Purification of alpha-glycerophosphate dehydrogenase from Drosophila melanogaster.

A simple procedure has been devised for the purification of alpha-glycerophosphate dehydrogenase (EC 1.1.1.8) FROM Drosophila melanogaster. The method involves substrate elution of the enzyme from a carboxymethyl cellulose column, followed by salt elution from agarose-hexane-AMP and DEAE columns. The procedure requires only 3 days to complete, results in high yield, and preparations that appear homogeneous by several criteria. A subunit molecular weight of 31 700 was obtained by sodium dodecyl sulphate electrophoresis in 10% acrylamide gels. This value is half that published for the native enzyme, confirming the homodimeric structure of this enzyme suggested by genetic evidence.

Animals↗
PubMed1975

The characterization of multiple forms of kynurenine formidase in Drosophila melanogaster.

Two enzymic forms of kynurenine formamidase (EC 3.5.1.9) from Drosophila melanogaster were separated and partially purified by pH fractionation, (NH4) 2SO4 fractionation and Sephadex G-75 gel filtration. The enzymes were also separated by DEAE-cellulose ion-exchange chromatography and distinguished by their different rates of thermal inactivation. The multiple forms are termed formamidase I and formamidase II. The molecular weight of formamidase I as measured by Sephadex G-75 chromatography is 60 000 and that of formamidase II is 31 000. The pH optima are broad, ranging between 6.7 and 7.8 for formamidase I and 6.5 and 8.0 for formamidase II. The apparent Km values are 5-10(-3) and 0.83-10(-3) M, resepctively. The possibility that formamidase II is an active subunit of formamidase I is discussed, although neither enzyme will convert to the other when separated and rechromatographed. Eight organisms were tested for the presence or absence of multiple forms of formamidase. Drosophila melanogaster and Drosophila virilis have both enzymes; cow, chicken, yeast and housefly have formamidase I only, and mouse and frog have formamidase II only.

Amidohydrolases↗
PubMed1975

Transport defects as the physiological basis for eye color mutants of Drosophila melanogaster.

Kynurenine-H3 transport and conversion to 3-hydroxykynurenine were studied in organ culture using the Malpighian tubules and developing eyes from wild type and the eye color mutants w, st, ltd, ca, and cn of Drosophila melanogaster. Malpighian tubules from wild type have the ability to concentrate kynurenine and convert it to 3-hydroxykynurenine. The tubules from w, st, ltd, and ca are deficient in the ability to transport kynurenine, as are the eyes of the mutants w, st, and ltd. This defect in kynurenine transport provides a physiological explanation for the phenotypic properties of the mutants. The relationship of these measurements to previous observations on these eye color mutants is discussed and the transport defect hypothesis is consistently supported. We have concluded that several of the eye color mutants in Drosophila are transport mutants.

Animals↗
PubMed1973

Developmental and genetic studies on kynurenine hydroxylase from Drosophila melanogaster.

The level of kynurenine hydroxylase was measured throughout the development of wild type and the eye color mutants v, cn, st, ltd, cd, kar, w, ca, bri and p(P) of Drosophila melanogaster. In all cases except cn a bimodal distribution of enzyme activity during development was observed. Activity is initially detectable in second instar. A maximum is reached in early third instar. Activity declines prior to puparium formation. Shortly after pupation, activity rises dramatically to reach a maximum about five times the peak larval level. Maximum activity persists for a short time, and then falls sharply prior to emergence. No activity is detectable in cn, cn(3), or cn(35K). In pupae which have zero, one, two or three doses of the cn(+) allele, activity is proportional to the number of the + alleles. This provides further evidence that the cn locus contains the structural gene for kynurenine hydroxylase. Kynurenine hydroxylase is a useful gene product for studying the events of imaginal disc differentiation.

Alleles↗
PubMed1968

Assay systems for the study of gene function. 2 assay systems, the syntheses of RNA and protein, are described; their virtues and drawbacks are discussed.

The study of genetic regulatory mechanisms operating in plants and animals is of paramount importance in contemporary biology. A precise understanding of the mechanisms that underlie normal cellular differentiation is a prerequisite for understanding neoplastic transformation and genetic disease. At present, we are not aware of a single assay system that can give answers to all questions we are already able to pose. Studies of RNA synthesis are valuable because they provide a direct measurement of transcriptional activity. But these studies remain incomplete until we succeed in unraveling the metabolic roles of the molecules whose synthesis we study. In this respect, the study of enzyme synthesis represents a better defined assay system, although the interpretation of observed fluctuations in synthetic rates is made difficult by the many steps that intervene between the genes and their finished protein products. We propose that a combination of protein biosynthetic and cytogenetic analysis is a promising assay system for further investigation.

Alcohol Oxidoreductases↗