scholarly journals An impedimetric determination of alkaline phosphatase activity based on the oxidation reaction mediated by Cu2+ bound to poly-thymine DNA

RSC Advances ◽  
2018 ◽  
Vol 8 (20) ◽  
pp. 11241-11246 ◽  
Author(s):  
Joon Young Lee ◽  
Jun Ki Ahn ◽  
Ki Soo Park ◽  
Hyun Gyu Park
Keyword(s):  
Alkaline Phosphatase ◽  
Ascorbic Acid ◽  
Phosphatase Activity ◽  
Modified Electrode ◽  
Alkaline Phosphatase Activity ◽  
Oxidation Reaction ◽  
Accurate Determination ◽  
Alp Activity ◽  
Mediated Oxidation

A novel impedimetric assay for the accurate determination of alkaline phosphatase (ALP) activity is developed based on the Cu2+-mediated oxidation of ascorbic acid on a poly-thymine DNA-modified electrode.

A MnO2nanosheets–o-phenylenediamine oxidative system for the sensitive fluorescence determination of alkaline phosphatase activity

2018 ◽  
Vol 10 (44) ◽  
pp. 5341-5346 ◽  
Author(s):  
Xionghong Tan ◽  
Zheng Li ◽  
Yanlin Du ◽  
Aixian Zheng ◽  
Yongyi Zeng ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Alp Activity ◽  
Fluorescence Determination ◽  
Oxidative System

A MnO2nanosheets–o-phenylenediamine (OPDA) oxidative system was developed for detecting ALP activity selectively, sensitively and conveniently.

A sensitive dual colorimetric and fluorescence system for assaying the activity of alkaline phosphatase that relies on pyrophosphate inhibition of the peroxidase activity of copper ions

The Analyst ◽  
2014 ◽  
Vol 139 (18) ◽  
pp. 4691-4695 ◽  
Author(s):  
Ki Soo Park ◽  
Chang Yeol Lee ◽  
Hyun Gyu Park
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Peroxidase Activity ◽  
Copper Ions ◽  
Accurate Determination ◽  
Highly Sensitive ◽  
Optical Assay

A novel and highly sensitive optical assay for the accurate determination of alkaline phosphatase activity is developed by utilizing the peroxidase activity of Cu2+ ions.

Alkaline phosphatase activity from human osteosarcoma cell line SaOS-2: an isoenzyme standard for quantifying skeletal alkaline phosphatase activity in serum.

1989 ◽  
Vol 35 (2) ◽  
pp. 223-229 ◽  
Author(s):  
J R Farley ◽  
E Kyeyune-Nyombi ◽  
N M Tarbaux ◽  
S L Hall ◽  
D D Strong
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Cell Lines ◽  
Alkaline Phosphatase Activity ◽  
Osteosarcoma Cell ◽  
Kinetic Assay ◽  
Human Osteosarcoma ◽  
Alp Activity ◽  
Human Osteosarcoma Cell ◽  
Skeletal Alkaline Phosphatase

Abstract Earlier we described a kinetic assay for quantifying skeletal alkaline phosphatase (ALP) isoenzyme activity in serum. The precision of the assay depends on including ALP standards for the skeletal, hepatic, intestinal, and placental isoenzymes. We wondered whether human osteosarcoma cells could provide an efficient alternative to human bone or Pagetic serum as a source of the skeletal ALP standard. ALP activities prepared from five human osteosarcoma cell lines were compared with a bone-derived ALP standard with respect to heat stability and sensitivity to chemical effectors. Two of the cell lines (SaOS-2 and TE-85) contained ALP activities that resembled the bone-derived standard. We selected SaOS-2 cells for additional evaluation (as a potential source of isoenzyme standard), because they contained 40-50 times more ALP activity than did the TE-85 cells. To include the SaOS-2 cell-derived ALP activity in the quantitative isoenzyme assay, we diluted the enzyme in a solution containing heat-inactivated (i.e., ALP-negative) human serum. Surprisingly, this dilution caused a 60-125% increase in maximum enzyme activity. In the quantitative assay of ALP isoenzyme in serum, the SaOS-2 derived ALP was indistinguishable from the serum skeletal ALP standard, with respect to the above criteria and assay variations. Evidently ALP from SaOS-2 cells is suited as a standard for measuring skeletal ALP activity in this assay.

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