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At least 433 records · Page 24Linked to original sources
PubMed1991

Evolution of the dec-1 eggshell locus in Drosophila. I. Restriction site mapping and limited sequence comparison in the melanogaster species subgroup.

We have analyzed approximately 18 kb of DNA in and upstream of the defective chorion-1 (dec-1) locus of the eight known species of the melanogaster species subgroup of Drosophila. The restriction maps of D. simulans, D. mauritiana, D. sechellia, D. erecta, and D. orena are shown to have basically the restriction map of D. melanogaster, whereas the maps of D. teissieri and D. yakuba were more difficult to align. However, the basic amount of DNA and sequence arrangement appear to have been conserved in these species. A small deletion of varying length (65-200 bp) is found in a repeated sequence of the central transcribed region of D. melanogaster, D. simulans, and D. erecta. Restriction site mapping indicated that the dec-1 gene is highly conserved in the melanogaster species subgroup. However, sequence comparison revealed that the amount of nucleotide and amino acid substitution in the repeated region is much larger than in the 5' translated region. The 5' flanking region showed noticeable restriction site polymorphisms between species. Based on calculations from the restriction maps a dendrogram was derived that supports earlier published phylogenetic relationships within the melanogaster species subgroup except that the erecta-orena pair is placed closer to the melanogaster complex than to D. teissieri and D. yakuba.

Amino Acid Sequence↗
PubMed1996

Complex carbohydrates in shell precursor globules of the vitellarium and at the eggshell of Hymenolepis microstoma (Cestoda).

The vitellocytes of Hymenolepis microstoma contain protein globules as building material for the shell of egg cocoons. Complex carbohydrates were detected as an additive component, dispersed in the matrix of the shell globules. Similar glycans were found at newly formed shells, suggesting that these molecules are provided by the vitellocytes. The glycans remained associated with the surface of mature eggs. Carbohydrate residues, characterized using gold-labeled lectins, were N-acetylglucosamine, galactose, or the N-acetyllactosamine sequence of these residues and N-acetylgalactosamine, whereas glucose, mannose, and fucose were not demonstrable. The glycans scarcely stained with periodic acid-Schiff and, thus, seem to have few diols, and they did not bind cationic dye, indicating that they are not glycosaminoglycans. Since they occur in significant amounts, the glycans may have fundamental, as yet undetermined function(s) in the formation of the shells and/or interactions of the cocoons with the host.

Animals↗
PubMed2006

Identification of eggshell membrane proteins and purification of ovotransferrin and beta-NAGase from hen egg white.

Exposure of selected Gram-positive and Gram-negative bacterial pathogens to egg shell membranes (ESM) significantly reduced their thermal resistance and/or inactivated cells. Although the components responsible for this antibacterial activity have not been conclusively identified, several proteins associated with the ESM activity have been identified including beta-N-acetylglucosaminidase, lysozyme and ovotransferrin, with each displaying varying degrees of antibacterial activity. Numerous attempts to purify active fractions of beta-N-acetylglucosaminidase, lysozyme and ovotransferrin from the ESM proved somewhat limited; however, hen egg white (HEW) beta-N-acetylglucosaminidase was purified using a two-step chromatographic procedure, isoelectric focusing followed by cation exchange chromatography. Pure fractions of ovotransferrin were also obtained in the process. SDS-PAGE electrophoresis and Matrix-Assisted Laser Desorption Time-of-Flight Mass Spectrometry were then used to partially characterize the individual protein components. Purified protein fractions such as these will be required in order to fully elucidate the mechanism responsible for the antimicrobial properties associated with the ESM.

Acetylglucosaminidase↗
PubMed1985

Synergistic effects of 1,25(OH)2D3 and 24,25(OH)2D3 on duodenal CaBP in rachitic chicks and on eggshell weight in Japanese quails.

The role of 24,25(OH)2D3 in calcium homeostasis is still controversial. In the present study the administration of low doses of 1,25(OH)2D3 and of higher doses of 24,25(OH)2D3 either alone or in conjunction with each other, were studied in rachitic chicks and in Japanese quails. Whereas 24,25(OH)2D3 alone had no significant effect on duodenal CaBP and on alkaline phosphatase in chick serum, it increased the influence of 1,25(OH)2D3 on these two parameters strongly. Also, when 1,25(OH)2D3 and 24,25(OH)2D3 were given simultaneously to Japanese quails, calcium excretion via the egg shell was clearly higher than when either metabolite had been administered alone. These results indicate that 1,25(OH)2D3 and 24,25(OH)2D3 exert a strong synergistic effect in rachitic animals.

24,25-Dihydroxyvitamin D 3↗