Cholinesterase, acid phosphatase, and phospholipase C ofPseudomonas aeruginosa under hyperosmotic conditions in a high-phosphate medium

1994 ◽  
Vol 28 (2) ◽  
pp. 71-76 ◽  
Author(s):  
Teresita A. Lisa ◽  
Cesar H. Casale ◽  
Carlos E. Domenech
1965 ◽  
Vol 24 (2) ◽  
pp. 235-251 ◽  
Author(s):  
Joachim R. Sommer ◽  
Jacob J. Blum

The localization of induced and constitutive acid phosphatase activity in Euglena was studied by light and electron microscopy, using two different cytochemical methods. Cells grown in high phosphate medium have constitutive acid phosphatase activity in three regions: in the Golgi complex, around the paramylum bodies, and in the peri-reservoir vesicles. Cells that have formed an induced acid phosphatase by exposure to a phosphate-deficient medium have, in addition to the constitutive activity localized exactly as in the uninduced cell, a strong activity in the pellicle. The induced activity is not uniformly distributed over the pellicle, but is localized at the notch of each pellicle complex, near a group of about four fibrils and near a characteristic vesicle of the endoplasmic reticulum. In the cytostome, where fission begins during division, there is an alternation of large and small pellicle complexes, both of which have induced phosphatase activity. A similar alternation is seen over the entire pellicle of dividing cells.


1971 ◽  
Vol 18 (2) ◽  
pp. 153-166 ◽  
Author(s):  
Jane North ◽  
D. Lewis

SUMMARY1.Coprinus lagopusproduces two non-specific phosphatases: a constitutive acid phosphatase, and an alkaline phosphatase which is repressed during growth on media with a high inorganic phosphate concentration.2. The alkaline phosphatase is also repressed whenCoprinusis grown on an organic phosphate source; but if the acid phosphatase is selectively inhibited by fluoride the alkaline phosphatase is de-repressed and growth is comparable to that observed on an inorganic phosphate source.3. Alkaline phosphatase is not repressed in aerial mycelium or sporophores even when grown on high phosphate medium.4. Mutants altered in their capacity to synthesize alkaline phosphatase were selected from two compatible wild-type strains, H2 and H5.5. Mutants producing a higher level of alkaline phosphatase than wild-type (‘regulator’ mutants) fall into four (or possibly five) complementation groups. Assuming five separate genes, two pairs are linked; the remaining one is independent and on another chromosome.6. Mutants deficient in alkaline phosphatase synthesis fall into at least three groups. They were tested for linkage to ‘regulator’ loci but so far there is no evidence of this.


1985 ◽  
Vol 5 (1) ◽  
pp. 248-252
Author(s):  
Y Kaneko ◽  
Y Tamai ◽  
A Toh-e ◽  
Y Oshima

A DNA fragment bearing the PHO8 gene, which encodes repressible alkaline phosphatase of Saccharomyces cerevisiae, was cloned. Northern hybridizations with the PHO8 DNA as probe indicated that the PHO8 transcript is 1.8 kilobases in length and is more abundant in cells grown in low-phosphate medium than in high-phosphate medium. The pho9 mutant, whose phenotype is defective in the activity of repressible alkaline phosphatase, produced as much of the PHO8 transcript as did the PHO9+ cells. Hence, the PHO9 product should act at the post-transcriptional level. The pho4 mutant could not derepress the PHO8 transcript, whereas the pho80 mutant could, irrespective of the amount of Pi in the medium, as has been suggested by genetic study.


1985 ◽  
Vol 5 (1) ◽  
pp. 248-252 ◽  
Author(s):  
Y Kaneko ◽  
Y Tamai ◽  
A Toh-e ◽  
Y Oshima

A DNA fragment bearing the PHO8 gene, which encodes repressible alkaline phosphatase of Saccharomyces cerevisiae, was cloned. Northern hybridizations with the PHO8 DNA as probe indicated that the PHO8 transcript is 1.8 kilobases in length and is more abundant in cells grown in low-phosphate medium than in high-phosphate medium. The pho9 mutant, whose phenotype is defective in the activity of repressible alkaline phosphatase, produced as much of the PHO8 transcript as did the PHO9+ cells. Hence, the PHO9 product should act at the post-transcriptional level. The pho4 mutant could not derepress the PHO8 transcript, whereas the pho80 mutant could, irrespective of the amount of Pi in the medium, as has been suggested by genetic study.


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