Sodium 2-naphthyl hydrogen phosphate

Sodium 2-naphthyl hydrogen phosphate Structure
Sodium 2-naphthyl hydrogen phosphate structure
Common Name Sodium 2-naphthyl hydrogen phosphate
CAS Number 14463-68-4 Molecular Weight 246.132
Density N/A Boiling Point N/A
Molecular Formula C10H8NaO4P Melting Point N/A
MSDS Chinese USA Flash Point N/A
Symbol GHS07
GHS07
Signal Word Warning

Bovine kidney low molecular weight acid phosphatase: FMN-dependent kinetics.

Biochem. Mol. Biol. Int. 41(6) , 1201-8, (1997)

A low molecular weight bovine kidney acid phosphatase, electrophoretically homogeneous and with a relative molecular mass of 17.8 kDa, was used in this work. Among the various substrates tested, FMN was found to be the most effective, at pH 7.0. Distinct acti...

Restoration of potent protein-tyrosine phosphatase activity into the membrane-distal domain of receptor protein-tyrosine phosphatase alpha.

Biochemistry 38(3) , 914-22, (1999)

Most transmembrane, receptor-like protein-tyrosine phosphatases (RPTPs) contain two cytoplasmic catalytic protein-tyrosine phosphatase (PTP) domains, of which the membrane-proximal domain, D1, contains the majority of the activity, while the membrane-distal d...

Inhibition of bovine kidney low molecular mass phosphotyrosine protein phosphatase by uric acid.

J. Enzyme Inhib. Med. Chem. 17(5) , 345-50, (2002)

Uric acid inhibited 50% of the activity of bovine kidney low molecular mass phosphotyrosine protein phosphatase at concentrations of 1.0, 0.4, 1.3, and 0.2 mM, respectively for p-nitrophenyl phosphate (p-NPP), flavine mononucleotide, beta-naphthyl phosphate a...

Importance of assay conditions in visualization and quantitation of serum alkaline phosphatase isoenzymes separated by electrophoresis.

Scand. J. Clin. Lab. Invest. 59(8) , 593-606, (1999)

The importance of separation and identification of serum alkaline phosphatase (ALP; E.C. 3.1.3.1) fractions/isoenzymes has been frequently reported. Each serum ALP fraction/isoenzyme quantitation has both practical and theoretical importance. In the present w...