Fluorescence Resolution of the Intrinsic Tryptophan Residues of Bovine Protein Tyrosyl Phosphatase
Open Access
- 1 February 1995
- journal article
- Published by Elsevier
- Vol. 270 (8) , 3809-3815
- https://doi.org/10.1074/jbc.270.8.3809
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Luminescence studies with trp repressor and its single-tryptophan mutantsBiochemistry, 1993
- 1002 Protein Phosphatases?Annual Review of Cell Biology, 1992
- Dominant forces in protein foldingBiochemistry, 1990
- Assignment of the heterogeneous static and time-resolved tryptophan fluorescence of 3-phosphoglycerate kinaseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1989
- Phase-resolved spectral measurements with several two tryptophan containing proteinsBiochemistry, 1987
- The human red cell acid phosphatase is a phosphotyrosine protein phosphatase which dephosphorylates the membrane protein band 3Biochemical and Biophysical Research Communications, 1986
- A major phosphotyrosyl-protein phosphatase from bovine heart is associated with a low-molecular-weight acid phosphataseArchives of Biochemistry and Biophysics, 1985
- Inorganic phosphate determination in the presence of a labile organic phosphate: Assay for carbamyl phosphate phosphatase activityAnalytical Biochemistry, 1983
- Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studiesBiochemistry, 1976
- FLUORESCENCE AND THE LOCATION OF TRYPTOPHAN RESIDUES IN PROTEIN MOLECULESPhotochemistry and Photobiology, 1973