Biomedical subjects

D R Frohlich

Publications and source records attributed to D R Frohlich.

9 recordsLinked to original sources

PubMed1996

Mitochondrial cytochrome C oxidase subunit I of Manduca sexta and a comparison with other invertebrate genes.

A cDNA encoding mitochondrial cytochrome c oxidase subunit I (mt COI) from Manduca sexta (Lepidoptera: Sphingidae) was cloned and sequenced. AT (adenine-thymine) content is high and codon usage is biased and likely reflects the role of mt COI in electron transport. The encoded protein is 514 amino acids long, contains seven invariant His residues observed in COIs in all organisms and would be predicted to be composed of 12 transmembrane regions.

Amino Acid Sequence↗

PubMed1995

Characterization and distribution of esterase electromorphs in the whitefly, Bemisia tabaci (Genn.) (Homoptera: Aleyrodidae).

Esterase profiles were examined for over 40 populations of the whitefly, Bemisia tabaci, obtained from native and cultivated plant hosts worldwide. Twelve unique electromorphs were identified from distinct populations concentrated largely in Central America, Africa, and India. One electromorph, type B, has recently been proposed as a separated species, Bemisia argentifolii, and has recently spread throughout much of the world. When considered with evidence from mating studies and the ability to induce phytotoxic disorders (squash silverleaf disorder), our data suggest that the single taxon Bemisia tabaci may actually represent a species complex.

Alleles↗

PubMed1994

Codon usage patterns among genes for lepidopteran hemolymph proteins.

Patterns in codon usage were examined for the coding regions of the 23 known lepidopteran hemolymph proteins. Coding triplets are GC rich at the third position and a significant linear relationship between GC content of silent and nonsilent (replacement) sites was demonstrated. Intron GC content was significantly lower than in coding regions and no relationship between intron GC content and the same at silent and nonsilent sites was found. Though hemolymph proteins are all produced by the same tissue--fat body--significantly less bias was observed when all moth sequences were pooled than when sequences of the two major species were analyzed separately, as predicted by the genome hypothesis. In cases where no statistically significant bias was observed, polar or acidic/basic amino acids were almost exclusively involved. Calculation of codon adaptation indices (CAI) was of limited value in quantifying the degree of codon bias and probably reflects the complexity of multicellular-organism life cycles and the changing patterns of gene expression over different developmental stages.

Animals↗

PubMed1993

Mediterranean fruit fly, Ceratitis capitata (Wiedemann), mitochondrial DNA: genes and secondary structures for six t-RNAs.

The polymerase chain reaction was used to amplify six mitochondrial t-RNAs for Ala, Arg, Asn, Ser, Glu and Phe between genes for mitochondrial NADH dehydrogenases 3 and 5. With respect to Drosophila yakuba the gene order and direction of transcription is completely conserved. Analysis of secondary structure shows complete conservation of the anticodon loops but a number of differences in the dihydrouridine and T psi C loops with respect to Drosophila. However, differences are such that tertiary interactions that stabilize stacking are preserved. The use of the reported sequence in combination with PCR to explore population variability is discussed.

Animals↗

PubMed1993

Polymorphic cDNAs encode for the methionine-rich storage protein from Manduca sexta.

By cDNA cloning and sequencing we have shown that Manduca sexta larvae produce three very closely related methionine-rich storage proteins, MMR1, MMR2 and MMR3. Out of 2256 nucleotides in the coding region, the cDNAs differ by at most twenty-one bases and this leads to a single amino acid difference between MMR1 and MMR2, and between MMR2 and MMR3, whereas MMR1 and MMR3 differ by two amino acids. Using both distance and parsimony methods, similarities between the M. sexta and Bombyx mori methionine-rich and arylphorin storage proteins were examined. Homologous proteins from the two species tend to be more closely related than are the two classes of storage proteins in a single species.

Amino Acid Sequence↗

PubMed1993

p-Nitrophenylacetate hydrolysis by honey bee esterases: kinetics and inhibition.

1. The kinetics and inhibition of p-nitrophenylacetate hydrolysis by cytosolic esterases of 1-day old female honey bees, Apis mellifera L., were studied. 2. The calculated values obtained were Km = 2.27 x 10(-5)M and Vmax = 2.48 x 10(-8) mol/s per mg protein. 3. The inhibition mechanisms examined for four organophosphorus insecticides were highly competitive in nature and based on competitive inhibition coefficients the order of toxicity was naled > dichlorvos > cis-mevinphos = trans-mevinphos. 4. Comparisons are made with the alfalfa leafcutting bee, Megachile rotundata (Fab).

Animals↗

PubMed1991

Peptide amphipathy: a new strategy in design of potential insecticides.

A 30-residue peptide [YAA(KALA)6LAA] with an amphipathic helix repeat unit of Lys-Ala-Leu-Ala (KALA) was synthesized as both the L- and the D-isomer. The peptide was shown to form alpha-helices and lyse lipid vesicles in a pH dependent fashion. The calculated helical amphipathic moment is +1.19 kcal/residue and the mean residue hydrophobicity is +0.4 kcal/residue. The formation of alpha-helices as the pH is increased is similar to poly-lysine, yielding a pK 10.2. Though not toxic when fed to insects, KALA killed Spodoptera frugiperda cells at low doses and Manduca sexta larvae when injected.

Amino Acid Sequence↗

PubMed1990

Esterase isozymes in a solitary bee, Megachile rotundata (Fab.): characterization, developmental multiplicity, and adult variability.

This study describes the biochemical characterization and genetic variation of cytosolic esterases in the alfalfa leafcutting bee, Megachile rotundata (Fab.). Esterase isozymes were separated by nondenaturing polyacrylamide gel electrophoresis and isoelectric focusing and characterized by inhibition with eserine sulfate, EDTA, paraoxon, and p-hydroxymercuribenzoate. Based on inhibition patterns and substrate specificity, there are major differences between adults and immature forms and more subtle differences between male and female adults. M. rotundata esterases are largely organophosphate sensitive and the two major adult allozymes were highly variable within the population examined. Differences in esterase expression between life stages with respect to niche and the occurrence of diploid males are discussed.

Animals↗

PubMed1990

The kinetics and inhibition of p-nitrophenylacetate-hydrolysing esterases in a solitary bee, Megachile rotundata (Fab.).

1. The kinetics and inhibition of p-nitrophenylacetate hydrolysis by cytosolic esterases of female alfalfa leafcutting bees, Megachile rotundata (Fab.) was examined. 2. For p-nitrophenylacetate, the Km = 1.24 x 10(-4) M and Vmax = 2.29 x 10(-9) mol/s per mg protein. 3. Regarding four organophosphate insecticides, the mechanism of inhibition in all cases was mixed (competitive and uncompetitive) and, based on inhibition constants, the order of toxicity was naled greater than paraoxon greater than trichlorfon greater than oxydemeton methyl. 4. Comparisons are made to the honey bee, Apis mellifera.

Animals↗