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Phosphate-binding tag : A new tool to visualize phosphorylated proteins

open access: yesPhosphate-binding tag : A new tool to visualize phosphorylated proteins
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Phosphate binding protein as the biorecognition element in a biosensor for phosphate

Sensors and Actuators B: Chemical, 2004
This work explores the potential use of a member of the periplasmic family of binding proteins, the phosphate binding protein (PBP), as the biorecognition element in a sensing scheme for the detection of inorganic phosphate (Pi). The selectivity of this protein originates from its natural role which, in Escherichia coli, is to serve as the initial ...
Sapna Deo, Sylvia Daunert
exaly   +3 more sources

Immunoblot detection of pyridoxal phosphate binding proteins in liver and hepatoma cytosolic extracts

Biochemical and Biophysical Research Communications, 1983
A monoclonal antibody, highly selective for the 5'-phosphopyridoxyl group, can be used to detect cytosolic pyridoxal-5'-phosphate binding proteins by an immunoblot procedure. This technique, when applied to sodium borohydride-treated cytosolic extracts obtained from normal rat liver at various stages of development as well as several liver-derived ...
John Cidlowski   +2 more
exaly   +3 more sources

Phosphate Binding by a Myeloma Protein

Acta Medica Scandinavica, 1987
ABSTRACT. A patient with IgG kappa myeloma had markedly elevated serum phosphate concentrations but no clinical features of hyperphosphataemia. The hyperphosphataemia was due to a high phosphate per protein unit than normal IgG.
T, Pettersson   +4 more
openaire   +2 more sources

The phosphate-binding protein of Escherichia coli

Biochimica et Biophysica Acta (BBA) - Biomembranes, 1970
Abstract 1. 1. Escherichia coli contains a phosphate-binding protein, in amounts exceeding 2 · 104 molecules per cell. Over 80% of this protein is released by osmotic shock. 2. 2. The phosphate-binding protein has been purified and found to have a molecular weight of 42 000. There is no evidence of subunits or aggregation. 3. 3.
N. Medveczky, H. Rosenberg
openaire   +1 more source

A Dynamical Investigation of Acrylodan-Labeled Mutant Phosphate Binding Protein

Analytical Chemistry, 1998
The static and dynamical behavior of a fluorescently labeled mutant of the Escherichia coli periplasmic phosphate binding protein (PBP) was investigated through steady-state and time-resolved fluorescence spectroscopy. As a means of developing a biorecognition element for inorganic phosphate (P(i)), alanine-197 of PBP was replaced with a cysteine. This
J S, Lundgren   +3 more
openaire   +2 more sources

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