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A Malacrida

Publications and source records attributed to A Malacrida.

12 recordsLinked to original sources
PubMed2002

Microsatellite analysis reveals remating by wild Mediterranean fruit fly females, Ceratitis capitata.

Accurate estimates of remating in wild female insects are required for an understanding of the causes of variation in remating between individuals, populations and species. Such estimates are also of profound importance for major economic fruit pests such as the Mediterranean fruit fly (Ceratitis capitata). A major method for the suppression of this pest is the sterile insect technique (SIT), which relies on matings between mass-reared, sterilized males and wild females. Remating by wild females will thus impact negatively on the success of SIT. We used microsatellite markers to determine the level of remating in wild (field-collected) Mediterranean fruit fly females from the Greek Island of Chios. We compared the four locus microsatellite genotypes of these females and their offspring. Our data showed 7.1% of wild females remated. Skewed paternity among progeny arrays provided further evidence for double matings. Our lowest estimate of remating was 3.8% and the highest was 21%.

Animals↗
PubMed1999

Tuberculosis and Pelger-Huët anomaly. Case report.

We describe a patient with pulmonary tuberculosis and a rare disturbance of leukocyte segmentation, known as "Pelger-Huët anomaly", which can be observed in various diseases such as malignancies and/or infections. The importance of this association is equivocal: some authors have related to the association the particular severity of tuberculosis or the death they observed; in the case reported we noted no evidence of such a relation, notwithstanding the presence of the homozygous form of the Pelger-Huët anomaly. We suggest therefore that, when Pelger-Huët anomaly is found, an underlying disease should be searched for; the course of this illness, however, might not be affected.

Adult↗
PubMed1998

Indications for a cost-saving policy in routine flow cytometry.

Flow cytometry has known a growing popularity in last decade as an intriguing research and diagnostic tool, favoured by the availability of newly developed monoclonal antibodies directed against cell surface antigens. Unfortunately, equipment and reagents costs are still prohibitive, and it does not allow a more widespread use of this technology. We realised that most producers suggest to add the same amount of reagents irrespective of the real number of target cells, and this is particularly true if the lysed whole blood technique is used. We investigated if an "individualized" concentration of reagents, based on the real number of MNC to be stained, could have allowed us to achieve qualitative satisfactory results with a concomitant reduction in costs. We studied four groups of individuals: 259 healthy subjects (239 blood donors and 20 volunteers) and 10 HIV+ patients. Our results suggest that lower amounts of reagents could be used, at least in some routinary cytometric analysis, simply following providers instructions (i.e. 1 microL of monoclonal antibody/1 x 10(5) MNC).

Adult↗
PubMed1997

Satisfactory recovery and viability of stem cells cryopreserved at high cell concentration.

Peripheral Blood Stem Cells (PBSC) are being extensively used in both oncology-haematology and in solid tumor therapy schedules. The latest generation of cell separators allow the collection of greater numbers of nucleated cells (NC) than is usually obtained in bone marrow transplantation (BMT) settings. Thus, larger volumes of components would be stored if the same NC concentration employed in BMT is to be used. In order to reduce large volume DMSO-infusion related side effects and to avoid storage problems, we froze components from 23 PBSC collections at higher NC concentrations, from 40-200 x 10(6)/mL. After 2-12 months of storage, we thawed the samples and determined if the high NC concentration had a detrimental effect on NC viability and on stem cell clonogenicity. No statistically significant differences emerged in regard to CFU-GM, CFU-GEMM and BFU-E percent recovery even at 200 x 10(6)/mL NC concentration.

Analysis of Variance↗
PubMed1992

Evidence for a genetic duplication involving alcohol dehydrogenase genes in Ceratitis capitata.

An Adh duplication is described in the medfly Ceratitis capitata. Evidence is presented for two separate Adh1 and Adh2 structural loci mapping at a distance of 0.49 recombination unit from each other. By deletion mapping the Adh region has been cytologically located near the free end of the left arm of the second chromosome within an area between 2C;3A segments of the polytene chromosome. The genetic analysis of the region around Adh has identified seven neighboring genes (Acon1, Mpi, Est6, Aox, Xdh, Mdh2, Lsp1) which identify the linkage group D. The orientation of loci with regard to the centromere sets the origin of the map of the left arm of the second chromosome close to the two Adh loci.

Alcohol Dehydrogenase↗
PubMed1983

6-Phosphogluconate dehydrogenase activity variants in Musca domestica L.: A further allele at the Pgd locus as proved by densitometric assay.

A new electrophoretic variant of 6-phosphogluconate dehydrogenase (6PGD) has been detected in flies of a laboratory Musca domestica strain. This variant is to be added to the two already described, PGD-A and PGD-B, identified by a fast-weak and a slow-thick electrophoretic band, respectively. The new variant, PGD-C, has the same mobility as PGD-A but provides a more intensely stained band; therefore it can be described as a fast-thick phenotype. The staining intensity of PGD-C is slightly lower than that of PGD-B. Genetic and densitometric tests have shown that the different levels of enzymatic activity of the two fast variants A and C are inherited as alternative genetic units, and they have been interpreted as one aspect of the phenotypic expression of two Pgd alleles, namely, PgdA and PgdC. These alleles determine both the rates of electrophoretic mobility (fast in both cases) and the levels of activity (low for A, strong for C; shown by weak or thick stained electrophoretic bands). Similarly, the two distinctive features of PGD-B, namely, slow mobility and high activity level, are always jointly inherited and appear as two pleiotropic aspects of the phenotype coded for by the PgdB allele. The PgdB/PgdC heterozygous flies provide a slightly asymmetrical three-banded zymogram, while the PgdA/PgdC combination leads to a single-banded pattern, showing the same mobility as the parents and an intermediate staining intensity. The quantitative analysis of enzyme activity of 6PGD zymograms, performed through densitometric methods, has led to the recognition of three different activity levels coded for by Pgd alleles, one of which, namely, PgdC, would not have been detected using electrophoretic methods alone.

Alleles↗
PubMed1979

6-phosphogluconate dehydrogenase in the housefly, Musca domestica L.:evidence for inheritable 6PGD polymorphism.

Two electrophoretic variants of the 6-phosphogluconate dehydrogenase (6 PGD) enzyme have been found in the WHO/IN/Musca domestica/l housefly laboratory strain. The patterns shown by Cellogel zone electrophoresis can be fully explained by the hypothesis of two codominant autosomal alleles. On this hypothesis, a specific Pgd locus has been postulated and the symbols PgdA and PgdB have been assigned to the two alleles causing the PGD-A and PGD-B phenotypes. The bands corresponding to the homozygous phenotypes PGD-A and PGD-B have different electrophoretic mobility and staining intensity; they can be described, respectively, as "fast-weak" and "slow-thick." The heterozygous phenotype PGD-AB gives a three-banded pattern, indicative of a dimeric structure for this enzyme; this pattern is asymmetrical. Heterozygous flies have been found both among wild-type strains of recent colonization and among old established laboratory colonies. Most strains are PgdB monomorphic; up to now only three strains have been PgdA monomorphic, all of them being multimarker strains. The Pgd locus has been traced to the housefly linkage group III.

Alleles↗
PubMed1978

Multiple forms with glucose 6-phosphate dehydrogenase activity in Musca domestica L. as revealed by electrophoresis on cellulose acetate gel.

Single newly emerged males of Musca domestica, WHO strain, usually show five electrophoretic bands of glucose 6-phosphate dehydrogenase (G6PD) activity. Of these five molecular forms, designated with Roman numerals in order from the origin, we have considered the first three: these have been characterized with respect to their substrate and coenzyme specificity and to their sensitivity to some sulfhydryl inhibitors. The data show band III to be G6P specific, nicotinamide adenine dinucleotide phosphate dependent and to be a type I enzyme according to Kamada and Hori's classification. Bands I and II, on the other hand, show wide substrate specificity and low sensitivity to the sulfhydryl inhibitors assayed. In addition, in the absence of an exogenous substrate and in the presence of nicotinamide adenine dinucleotide as a coenzyme, fairly weak bands, which can be ascribed to the so called "nothing dehydrogenase" effect, are seen in the position I and II. Nevertheless, the data reported do not allow a clear definition of the enzymatic type corresponding to bands I and II of G6PD activity.

Animals↗
PubMed1978

The in vitro conversion of a specific molecular form of glucose 6-phosphate dehydrogenase from Musca domestica L.

A nicotinamide adenine dinucleotide phosphate dependent glucose 6-phosphate dehydrogenase (G6PD), belonging to type I of Kamada and Hori's classification, is present on the zymograms of newly emerged males of Musca domestica. It is capable of undergoing tryptic degradation and being thus transformed into a different active enzymatic form, with some of its catalytic properties unchanged, but with different electrophoretic mobility. We show in this paper that this specific G6PD form of gut origin in M. domestica is not a tissue-specific enzyme, but rather a product of hydrolytic degradation by gut proteinases which act during the process of homogenization. Besides, the G6PD of type I in the housefly is shown to be sensitive to the "storage effect" and to protection by mercaptoethanol, contrary to its hydrolytic gut form which is not sensitive to these processes. In this connection, we discuss the possible reasons for these differences in behavior.

Animals↗
PubMedDate not supplied

6PGD in the housefly. Mapping of the Pgd locus in linkage group III of Musca domestica.

The Pgd locus, which codes the enzyme 6-phosphogluconate dehydrogenase (6PGD), has been located in linkage group III of Musca domestica L. near the morphological marker green eye (ge) at a distance of less than one recombination unit. Linkage relationships also were determined for Pgd and other markers of linkage group III. Loose linkages were recorded between the locus Pgd and the DDT resistant factor kdr. A linkage map of autosome 3 is given, showing the best characterized loci and the most accurate recombination frequencies.

Animals↗