Biophysical Journal 1995-04-01

A new method for the time-resolved measurement of phosphate release in permeabilized muscle fibers.

M A Ferenczi, Z H He, R K Chillingworth, M Brune, J E Corrie, D R Trentham, M R Webb

Index: Biophys. J. 68(4 Suppl) , 191S-192S; discussion 192S-193S, (1995)

Full Text: HTML

Abstract

A new method for the measurement of phosphate release in contracting and relaxed permeabilized muscle fibers is described. The assay is based on a genetically engineered phosphate-binding protein labeled with a coumarin fluorescent probe, which binds inorganic phosphate tightly and shows a fourfold increase in fluorescence upon binding. Measurements of Pi release on the millisecond time scale with sensitivity in the 10 microM range are obtained that provide new information about the relationship between ATP hydrolysis and force production.

Related Compounds

Related Articles:

A fluorescent sensor of the phosphorylation state of nucleoside diphosphate kinase and its use to monitor nucleoside diphosphate concentrations in real time.

2001-04-24

[Biochemistry 40(16) , 5087-94, (2001)]

Development of fluorescent biosensors for probing the function of motor proteins.

2007-04-01

[Mol. Biosyst. 3(4) , 249-56, (2007)]

Site-specific labeling of T7 DNA polymerase with a conformationally sensitive fluorophore and its use in detecting single-nucleotide polymorphisms.

2009-01-01

[Anal. Biochem. 384(1) , 136-44, (2009)]

The interaction between rac1 and its guanine nucleotide dissociation inhibitor (GDI), monitored by a single fluorescent coumarin attached to GDI.

1999-06-01

[Biochemistry 38(21) , 6879-86, (1999)]

Crystal structure of phosphate binding protein labeled with a coumarin fluorophore, a probe for inorganic phosphate.

1998-07-21

[Biochemistry 37 , 10381, (1998)]

More Articles...