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Biomedical subjects

R A Morton

Publications and source records attributed to R A Morton.

At least 55 records · Page 3Linked to original sources
PubMed1990

Radical retropubic prostatectomy. Improved anastomosis and urinary continence.

The striated urethral sphincter is the predominant muscular structure divided posteriorly during the apical dissection in radical prostatectomy. The authors have long realized the value of this maneuver in obtaining excellent apical surgical margins and in identifying the correct plane on the anterior surface of the rectum. Recently, they also have recognized the importance of incorporating this musculature into the vesicourethral anastomosis to fix the bladder neck and thus re-establish anatomic continuity. Identification of the striated urethral sphincter ranks in importance with elucidation of the anatomy of the dorsal vein complex and the anatomic identification of the neurovascular bundle in improving the patient's quality of life postoperatively.

Anastomosis, Surgical↗
PubMed1988

Genes controlling malathion resistance in a laboratory-selected population of Drosophila melanogaster.

The chromosomal locations of several genes responsible for increased malathion resistance in a laboratory-selected population of Drosophila melanogaster have been determined. These genes appear to be involved in the regulation of microsomal cytochrome P-450. A major gene on chromosome 2 (2-64) and at least two genes on chromosome 3 (near 3-58) control increased mixed function oxidase activity, and both larval and adult malathion resistance. Although the chromosome 2 locus was not associated with a significant increase in cytochrome P-450 content, SDS polyacrylamide gel electrophoresis of microsomal proteins detected increased silver staining of a polypeptide having a relative molecular mass (Mr) of about 52,000. Microsomes from strains carrying the chromosome 3 factors for resistance contained more cytochrome P-450 and increased amounts of two heme-staining protein bands (Mr = 50,000 and 54,000). The genes regulating these proteins were closely linked to striped at 3-62 and probably identical to the loci responsible for malathion resistance and increased mixed function oxidase activity. Other R genes on both chromosomes 2 and 3 as well as target resistance were required for the full expression of malathion resistance in the selected Drosophila population. Exposure of this Drosophila melanogaster population to malathion selected a polygenic system for the oxidative metabolism of insecticide.

Animals↗
PubMed1985

Biochemical properties, homology, and genetic variation of Drosophila "nonspecific" esterases.

The biochemical properties and tissue distribution of two major, soluble "nonspecific" esterases have been studied in Drosophila melanogaster, D. pseudoobscura, and related species. The "alpha-like" activity is due to a monomer enzyme (MW congruent to 60 kd) having a nonspecific tissue distribution, which was inhibited by p-hydroxymercuribenzoate (5 X 10(-4)M) plus eserine (1 X 10(-5)M) and was relatively unstable during polyacrylamide gel electrophoresis. Electrophoretograms of this enzyme could be enhanced by treating gels with beta-mercaptoethanol before staining. This procedure allowed the identification of a new alpha-esterase (Est-4) in D. pseudoobscura. The "beta-like" esterase activity (EC 3.1.1.1) is due to a dimer (MW congruent to 120 kd) in most Drosophila species. D. melanogaster and its siblings (D. simulans and D. mauritiana) were exceptions in which this enzyme had an unusual tissue distribution (increased activity in the male reproductive system) and was a monomer (MW congruent to 60 kd). Differences in the genetic variability of these esterases are discussed and interpreted by a population expansion model rather than by differences in biochemical properties of enzyme forms.

Animals↗
PubMed1982

The association between malathion resistance and acetylcholinesterase in Drosophila melanogaster.

The relationship between the 50% survival time for flies feeding on a malathion-containing medium and the activity of acetylcholinesterase (AChE) was determined for 15 isofemale lines of Drosophila melanogaster. A significant correlation was found (r = 0.28, P less than 0.05), with more resistant lines tending to have a lower level of AChE activity. An association between AChE and malathion resistance was also observed in a selection experiment. The AChE activity decreased in two of two populations selected for malathion resistance. AChE from these populations was altered in kinetic parameters (measured in crude head extracts) and electrophoretic mobility. Although the "resistant" AChE had a lower activity (Vm) on either a per milligram protein or a per individual basis, its apparent Km for acetylthiocholine was lower than that of "susceptible" AChE. Recombination mapping of both low activity and fast electrophoretic mobility localized these traits to the region of the structural locus (Ace) on the third chromosome. The AChE activity of flies heterozygous for a variety of Ace lesions (kindly provided by Dr. W. M. Gelbart) was consistent with this location. The changes in AChE were suggested to have been caused by selection of alleles at the Ace locus.

Acetylcholinesterase↗
PubMed1981

Selection for malathion-resistance in Drosophila melanogaster.

Results from a long-term selection experiment for malathion-resistance in Drosophila melanogaster are described. A polled population of 40 locally-caught, iso-female lines was exposed to increasing concentrations of malathion in the food at both a high selection intensity (MH) and a lower intensity (ML). The response was consistent with a polygenic system. Both adult and larval resistance increased in parallel. Changes in the dose-response curve of adults could be approximately described by a dose-modification factor. Larval resistance was more complex; both selected populations showed a maternal effect which could not be explained by sex-linked genes. Larval resistance in the selected populations behaved as a co-dominant trait with respect to the susceptible controls. Adult resistance was dominant in the ML and co-dominant in the MH population, suggesting that different genes conferring resistance were selected. The selection procedure also produced a developmental delay in both populations, dependent on malathion concentration, but present even in its absence.

Animals↗
PubMed1980

Variation in Drosophila acetylcholinesterase.

We examined the Canton-S strain of Drosophila melanogaster for electrophoretic variation of the enzyme acetylcholinesterase. The pattern of bands obtained (stained with acetylthiocholine) depended on age, sex, and tissue (i.e., head vs. body part and hemolymph). However, through mixing experiments, it was concluded that most of these apparent differences were due to modification of the enzyme by unknown substances located in the fly's body. The electrophoretic pattern of head acetylcholinesterase was altered so that it became characteristic of the body which was present during extraction. For example, when heads of D. melanogaster were homogenized in an extract from D. lebanonensis bodies, the characteristic AChse bands of melanogaster were absent and instead of the bands of lebanonensis were found. It was found that extraction of adult heads in 0.1 M potassium phosphate buffer alone or with a 2-min exposure to 1 mg/ml trypsin at 20 C gave the most reproducible results, independent of age and sex. Using these conditions, 25 strains of D. melanogaster and 30 strains of D. pseudoobscura were examined without finding any reproducible electrophoretic variant of acetylcholinesterase. In addition, 53 strains from 39 other Drosophila species produced a total of only six electrophoretic forms of the head enzyme. Additional electromorphs were found when whole flies were used, but these were not studied in detail because of the possibility that they could be due to postextraction modification.

Acetylcholinesterase↗
PubMed1977

Ion binding to lysine-modified derivatives of cytochrome c.

The effect of Cl- and K+ ions on the apparent equilibrium constant of the reaction between horse ferricytochrome c and potassium ferrocyanide was studied. Unmodified cytochrome was compared with two lysine-modified derivatives. One, guanidinated, had all lysyl groups converted to homoarginine (but retained the same positive charge); the other was trinitrophenylated at one lysine (measured spectrophotometrically). Both modified derivatives had a somewhat larger equilibrium constant in the reaction of the reduced protein with ferricyanide, but, unlike trifluoroacetylated cytochrome c (which has a negative charge), the redox properties were not dramatically different. The native protein and the lysine-modified cytochromes showed differential K+ binding in Tris-cacodylate buffer at constant ionic strength (0.003-0.005 M). More K+ was bound to ferrocytochrome c. This redox-linked binding, however, was unaffected by modification of lysine. All three derivatives also showed redox-linked differential Cl- ion binding (more Cl- ion was bount to ferricytochrome); however, in this case, the binding was reduced in the lysine-modified molecules. This was interpreted as loss of a single anion site. This anion site critically depends on one or a few lysines which are more reactive with trinitrobenzene sulfonate.

Binding Sites↗
PubMed1977

The oxidation of ferrocytochrome c in nonbinding buffer.

The apparent equilibrium constant and rate of oxidation was investigated for the reaction of cytochrome c with iron hexacyanide. It was found that if horse heart ferricytochrome c was exposed to ferricyanide (to oxidize traces of reduced protein) the cytochrome subsequently, even after extensive dialysis, had an apparent equilibrium constant different from that of electrodialyzed protein. The effect of ferricyanide ion apparently cannot be removed by ordinary dialysis. The ionic strength dependence of the apparent equilibrium constant and bimolecular oxidation rate constant was measured in the range 1--200 mM using Tris--cacodylate or potassium phosphate buffers at pH 7.0, and electrodialyzed horse heart cytochrome c. The oxidation reaction proceeded very rapidly. Extrapolated to zero ionic strength, kox (approximately 9 X 10(9) M-1 S-1) was about 7% of that calculated for a diffusion-limited reaction. Since the exposed heme edge occupies only the order of 3% of the surface area, electron transfer apparently results at nearly every collision with the active-site region. An effective charge of + 7.8 units was estimated for the oxidation reaction. The rate of oxidation of Pseudomonas aeruginosa c551 was much slower (kox at mu = 0 was the order of 6 X 10(3)), and was not consistent with diffusion-limited kinetics.

Animals↗