Results 121 to 130 of about 994 (158)
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The polyphosphatases of Aspergillus niger. I. The non-identity of metaphosphatase with apyrase and pyrophosphatase

Archives of Biochemistry and Biophysics, 1953
Abstract The following lines of evidence indicate that the metaphosphatase (MPase) of A. niger is distinct from apyrase and pyrophosphatase (PPase): 1. 1. The pH optimum for MPase is different from that for apyrase and PPase. 2. 2. When the mold is grown for periods of 3–4 weeks on synthetic medium it is found that MPase concentration varies ...
P S, KRISHMAN, , BAJAJ
openaire   +2 more sources

Survey of the occurrence of adenosine polyphosphatase in extracellular matrix of rat tissues

Histochemistry, 1991
The extracellular presence of adenosine polyphosphatase was investigated in a number of rat tissues. The enzyme was demonstrated in basement membranes of epithelial cells of duodenum, urinary bladder, tongue, choroid plexus, submandibular salivary gland, lung and kidney, as well as in basement membranes of capillaries in these tissues.
D Kalicharan, M J Hardonk, W W Bakker
exaly   +4 more sources

Polyphosphatase acitivities in the soluble fraction of mycelial homogenates of Pisolithus tinctorius

Agriculture, Ecosystems & Environment, 1990
Abstract Activities of acid phosphatase activities in the soluble fraction of Pisolithus tinctorius homogenates, cultured on media with or without Pi 100 μM were assayed using sodium polyphosphates. Phosphatase activities increased with decreasing lengths of polyphosphate chains.
Tillard, Pascal   +4 more
openaire   +2 more sources

[Escherichia coli membrane-bound polyphosphatase].

Biokhimiia (Moscow, Russia), 1976
A complex of polyphosphatase with E. coli membranes has been isolated and studied. It is shown by gel-filtration through G-200 Sephadex and centrifugation in sucrose concentration gradient that about 5% of polyphosphatase total content in cells is bound with the heterogenous fraction containing smooth membranes and the ribosome-membrane complex. On the
A I, Severin   +3 more
openaire   +1 more source

[Organelle specificity of yeast cell polyphosphatases].

Biokhimiia (Moscow, Russia), 1996
The properties of purified cell envelope polyphosphatase, polyphosphatase activities of vacuoles and cytosol fractions of the Saccharomyces cerevisiae yeast have been compared. The whole body of evidence presently available suggest that each of the compartments under study is equipped with its own polyphosphatase which differs from polyphosphatases of ...
I S, Kulaev   +3 more
openaire   +1 more source

[Isolation and properties of polyphosphatase of Neurospora crassa].

Molekuliarnaia biologiia, 1976
Polyphosphatase (polyphosphate-phosphohydrolase) has been isolated from mycelium of Neurospora crassa and purified to homogenous state. The enzyme is shown to be strictly specific to high molecular weight inorganic polyphosphates. Km for phosphate in polymeric form is 6.8-10(-4) M. The molecular weight of this enzyme is 50 000 +/- 3000.
A M, Umnov, N S, Umnova, I S, Kulaev
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[Characteristics of polyphosphatase activity of Saccharomyces cerevisiae cytosol].

Biokhimiia (Moscow, Russia), 1995
The cytosol fraction purified from cellular organelles was obtained from S. cerevisiae yeast cells. This cytosolic fraction contained a polyphosphatase activity comprising nearly 65% of such in the protoplast homogenate. The pH optimum of this activity was 6.5-7.5.
N A, Andreeva   +2 more
openaire   +1 more source

Yeast Polyphosphatases PPX1 and PPN1: Properties, Functions, and Localization

2016
The PPX1 and PPN1 genes of Saccharomyces cerevisiae encode the enzymes that hydrolyze inorganic polyphosphates (polyP) of different chain lengths including tripolyphosphate. They are divalent metal ion dependent. PPX1 is an exopolyphosphatase splitting Pi from polyP chain end.
Nadeshda Andreeva   +4 more
openaire   +1 more source

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