Induction of null-activity mutants for the acid phosphatase-1 gene in Drosophila melanogaster

1972 ◽  
Vol 6 (2-3) ◽  
pp. 205-216 ◽  
Author(s):  
John B. Bell ◽  
Ross J. MacIntyre ◽  
Allan P. Olivieri
Keyword(s):  
Drosophila Melanogaster ◽  
Acid Phosphatase

Recent findings in oogenesis of Drosophila melanogaster

Development ◽  
1977 ◽  
Vol 39 (1) ◽  
pp. 45-57
Author(s):  
F. Giorgi ◽  
J. Jacob
Keyword(s):  
Drosophila Melanogaster ◽  
Acid Phosphatase ◽  
Ovarian Development ◽  
Superficial Layer ◽  
Blood Proteins ◽  
Selective Hydrolysis ◽  
Internal Lining ◽  
Hydrolysis Of ◽  
Zinc Iodide ◽  
Yolk Platelet

The role played by the vitellogenic oocytes of Drosophila melanogaster in relation to the elaboration of material taken from the haemolymph is examined by ultrastructural cytochemistry. As revealed by the Gomori procedure, acid phosphatase occurs widely over the forming yolk platelets of the cortical and central ooplasm. A number of Golgi apparatuses in thecortical ooplasm are also positively stained with lead precipitates. With the proceeding of the ovarian development it becomes progressively more difficult to demonstrate cytochemically the enzyme over the yolk platelets. In stage 9–10 chambers the acid phosphatase is restricted to the so-called associated body, while the rest of the yolk platelet appears devoid of lead deposits. By using a osmium zinc iodide (OZ1) complex as a preferential staining method for the Golgi apparatus, it has been shown that, apart from the apparatus itself, a number of OZI deposits occur over the superficial layer of the forming yolk platelets. When mature yolk platelets are formed at later stages, the OZI deposits in the yolk platelets come to be restricted to the cap-like region of the superficial layer which contains the associated body. In vitellogenic oocytes, both the internal lining of the limiting membrane of the forming yolk platelets and the associated body of the mature yolk platelets react positively, to cytochemical methods to demonstrate carbohydrates. The present findings are interpreted as indicating the involvement of lysosomal enzymes in the process of maturation of the yolk material. The suggestion is also made that such an involvement is required to accomplish a selective hydrolysis of those blood proteins which have been taken in by vitellogenic oocytes along with yolk precursors.

Combined histochemical and x-ray microanalytical studies on the copper-accumulating granules in the mid-gut of larval Drosophila

1977 ◽  
Vol 26 (1) ◽  
pp. 201-215
Author(s):  
R.L. Tapp ◽  
A. Hockaday
Keyword(s):  
Drosophila Melanogaster ◽  
Acid Phosphatase ◽  
Energy Dispersive ◽  
X Ray ◽  
Gut Epithelium

The copper-containing granules in the mid-gut epithelium of larval Drosophila melanogaster were examined for acid phosphatase by combined histochemistry and energy-dispersive, X-ray microanalysis. After incubation, many of the granules were shown to contain simultaneously copper and sulphur (which are normal constituents), and lead and phosphorus (which are the detectable elements of the reaction product). Earlier work has been consolidated and extended and the evidence that the granules are formed as cytolysosomes is reviewed.

Regulation of acid phosphatase activity in the ovary of Drosophila melanogaster

1975 ◽  
Vol 47 (1) ◽  
pp. 196-205 ◽  
Author(s):  
John H. Postlethwait ◽  
Pat Gray
Keyword(s):  
Drosophila Melanogaster ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity

Position effect variegation of an acid phosphatase gene in Drosophila melanogaster

1984 ◽  
Vol 197 (3) ◽  
pp. 403-413 ◽  
Author(s):  
M. C. Frisardi ◽  
Ross J. MacIntyre
Keyword(s):  
Drosophila Melanogaster ◽  
Acid Phosphatase ◽  
Position Effect ◽  
Position Effect Variegation ◽  
Effect Variegation ◽  
Acid Phosphatase Gene

Latitudinal variation in octanol dehydrogenase and acid phosphatase allele frequencies in Drosophila melanogaster

1983 ◽  
Vol 65 (3) ◽  
pp. 191-196 ◽  
Author(s):  
J. G. Oakeshott ◽  
J. B. Gibson ◽  
D. A. Willcocks ◽  
G. K. Chambers
Keyword(s):  
Drosophila Melanogaster ◽  
Acid Phosphatase ◽  
Allele Frequencies ◽  
Latitudinal Variation ◽  
Octanol Dehydrogenase

THE GENETICS OF AN ACID PHOSPHATASE IN DROSOPHILA MELANOGASTER AND DROSOPHILA SIMULANS

Genetics ◽  
1966 ◽  
Vol 53 (3) ◽  
pp. 461-474
Author(s):  
Ross Mac Intyre
Keyword(s):  
Drosophila Melanogaster ◽  
Acid Phosphatase ◽  
Drosophila Simulans

Naturally occurring quantitative variants of acid phosphatase-1 in Drosophila melanogaster

1985 ◽  
Vol 23 (5-6) ◽  
pp. 465-482 ◽  
Author(s):  
Mitrick A. Johns ◽  
John H. Postlethwait
Keyword(s):  
Drosophila Melanogaster ◽  
Acid Phosphatase ◽  
Naturally Occurring

scholarly journals Purification and characterization of acid phosphatase-1 from Drosophila melanogaster.

1980 ◽  
Vol 255 (21) ◽  
pp. 10338-10343
Author(s):  
M.I. Feigen ◽  
M.A. Johns ◽  
J.H. Postlethwait ◽  
R.R. Sederoff
Keyword(s):  
Drosophila Melanogaster ◽  
Acid Phosphatase ◽  
Purification And Characterization

Intracellular and Extracellular Acid Hydrolase Activity in the Drosophila Melanogaster Ovary

1982 ◽  
Vol 40 ◽  
pp. 242-243
Author(s):  
Lawrence G. Altman ◽  
R. Witkus ◽  
G. M. Vernon
Keyword(s):  
Drosophila Melanogaster ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Osmium Tetroxide ◽  
Uranyl Acetate ◽  
Acid Hydrolase ◽  
Lead Citrate ◽  
Wild Type ◽  
Thin Sections

Ovaries from wild type Drosophila melanogaster were incubated for acid phosphatase activity (pH 5). Following fixation in either 3.0% or 6.0% glutaraldehyde prepared in 0.1M cacodyiate buffer. Post-fixation was done in 1.0% osmium tetroxide and tissues were subjected to a graded series of acetone and infiltrated with Epon-Araldite. Control tissues were incubated without the substrate, in this case Bglycerophosphate. Ultrastructural integrity was checked against tissue prepared by omitting the incubation period completely. Thin and semi-thin sections were cut on an LKB ultramicrotome. In some instances, observations were recorded without uranyl acetate and lead citrate counterstaining.

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