Abstract
Anacystis nidulans (Synechococcus) was maintained in a medium of low phosphate concentration (0.1 mM) and grew with a normal doubling time of 5 hrs at 30 degrees C. Such cultures had a normal pigment composition and alkaline phosphatase was detectable at low specific activities only. The onset of phosphate-limited growth occurred when the phosphate concentration in the medium fell to a value below 4 muM (the limit of accurate determination by the assay method used ) and resulted in increases in alkaline phosphatase activity, reaching a final 10 to 15 fold increase in specific activity after a period of several hours. Marked changes in the overall pigment composition occurred in this period of growth restriction. The addition of phosphate to such cultures resulted in a halt in synthesis of the enzyme and the restoration of normal pigmentation before growth resumed at the normal rate. Several oraganic phosphate esters could replace inorganic phosphate for growth and were also hydrolyzed by the partially purified enzyme, but growth rates were characteristically lower and the specific activity only 3 to 4 fold higher than in cultures grown in phosphate excess. Studies with the partially purified enzyme suggested that it differed in some of its properties from other alkaline phosphatases described in the literature.
MeSH Terms
Alkaline Phosphatase/antagonists & inhibitors,metabolism
Culture Media
Cyanobacteria/enzymology,growth & development,metabolism
Esters
Phosphates/metabolism
Photosynthesis
Pigments, Biological/analysis
Time Factors
Chemicals
Culture Media
Esters
Phosphates
Pigments, Biological
Alkaline Phosphatase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Ihlenfeldt M J
Gibson J
References (16)
16 references, click to expand
-
The determination of phosphorus and phosphatase with N-phenyl-p-phenylenediamine.
J Biol Chem. 1957 Mar;225(1):177-83
PMID: 13416228
-
A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. coli. I. Purification and characterization of alkaline phosphatase.
Biochim Biophys Acta. 1960 Mar 11;38:470-83
PMID: 13826559
-
Cytochemical localization of certain phosphatases in Escherichia coli.
J Bacteriol. 1970 Oct;104(1):529-42
PMID: 4319724
-
Metabolism of glucose by unicellular blue-green algae.
Arch Mikrobiol. 1972;87(4):303-22
PMID: 4629415
-
CO2 fixation and its regulation in Anacystis nidulans (Synechococcus).
Arch Microbiol. 1975;102(1):13-21
PMID: 235244
-
Genetic control of repression of alkaline phosphatase in E. coli.
J Mol Biol. 1961 Aug;3:425-38
PMID: 13725581
-
Alkaline phosphatase of Escherichia coli: a zinc metalloenzyme.
Biochemistry. 1962 May 25;1:373-8
PMID: 14487220
-
Phosphorus deficiency and phosphate uptake in the blue-green alga Anacystis nidulans.
Can J Microbiol. 1968 Apr;14(4):341-8
PMID: 5646835
-
Further studies on the induction of alkaline phosphatase by 5-bromodeoxyuridine in a hybrid line between mouse and Chinese hamster in culture.
Biochim Biophys Acta. 1972 May 16;264(3):497-507
PMID: 5063668
-
Relation between pigment content and photosynthetic characteristics in a blue-green algae.
J Gen Physiol. 1955 Sep 20;39(1):11-22
PMID: 13252232
-
Relationship between phosphates and alkaline phosphatase of Anabaena flos-aquae in continuous culture.
Arch Mikrobiol. 1971;80(2):147-53
PMID: 5001948
-
Influence of inorganic phosphate in the formation of phosphatases by Escherichia coli.
Biochim Biophys Acta. 1960 Mar 11;38:460-9
PMID: 13838951
-
Kinetic studies of pigment synthesis by non-sulfur purple bacteria.
J Cell Comp Physiol. 1957 Feb;49(1):25-68
PMID: 13416343
-
Nitrogen chlorosis in blue-green algae.
Arch Mikrobiol. 1969;69(2):114-20
PMID: 4986616
-
The incorporation and metabolism of glucose by Anabaena variabilis.
J Gen Microbiol. 1968 Dec;54(3):451-62
PMID: 4236986
-
Enhancement in the Blue-Green Alga, Anacystis nidulans.
Plant Physiol. 1964 Nov;39(6):938-46
PMID: 16656038