Establishment and characterization of tartrate-resistant acid phosphatase and alkaline phosphatase double positive cell lines

2001 ◽  
Vol 304 (3) ◽  
pp. 351-359 ◽  
Author(s):  
Riako Masuda ◽  
Hisako Sakiyama ◽  
Takashi Nonaka ◽  
Alvin Kwan ◽  
Koichi Nakagawa ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Cell Lines ◽  
Tartrate Resistant Acid Phosphatase ◽  
Double Positive ◽  
Double Positive Cell

scholarly journals Bone-Derived Serum Enzymes and Bone Density in Perimenopausal Caucasian Women

1993 ◽  
Vol 30 (2) ◽  
pp. 191-194 ◽  
Author(s):  
J D Johnston ◽  
S Koneru ◽  
T Kuwana ◽  
S B Rosalki
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Bone Density ◽  
Femoral Neck ◽  
Serum Levels ◽  
Bone Alkaline Phosphatase ◽  
Serum Enzymes ◽  
Tartrate Resistant Acid Phosphatase ◽  
Vertebral Bone ◽  
Caucasian Women

Serum levels of bone-origin alkaline phosphatase and of tartrate-resistant acid phosphatase were measured in Caucasian women aged 41–69 years who had volunteered for bone densitometry. Bone alkaline phosphatase and tartrate-resistant acid phosphatase were inversely correlated with vertebral bone density and with femoral neck bone density. Bone alkaline phosphatase and acid phosphatase were also significantly correlated, consistent with the concept of ‘coupling’ between osteoblast and osteoclast activity.

Biochemical characterization of the tartrate-resistant acid phosphatase of human spleen with leukemic reticuloendotheliosis as a pyrophosphatase.

1977 ◽  
Vol 23 (1) ◽  
pp. 89-94 ◽  
Author(s):  
K W Lam ◽  
L T Yam
Keyword(s):  
Acid Phosphatase ◽  
Biochemical Characterization ◽  
Normal Animal ◽  
Tartrate Resistant Acid Phosphatase ◽  
Animal Tissues ◽  
Human Spleen ◽  
Optimal Activity ◽  
Catalytic Function ◽  
Hydrolysis Of

Abstract A tartrate-resistant acid phosphatase was isolated from a human leukemic spleen by freeze-thawing in saline and purified by repeated chromatography on carboxymethyl-cellulose. The purified enzyme has a molecular weight of 64 000. It catalyzes the hydrolysis of inorganic and organic pyrophosphate as well as the phenolic ester of monoorthophosphate, with optimal activity between pH 5 and 6. However, there is no activity toward mono-orthophosphate esters of aliphatic alcohols. The present data have identified its catalytic function as a pyrophosphatase. However, it has properties different from the pyrophosphatase previously observed in normal animal tissues.

Characterization of the mouse tartrate-resistant acid phosphatase (trap) gene promoter

2009 ◽  
Vol 10 (4) ◽  
pp. 601-606 ◽  
Author(s):  
S.V. Reddy ◽  
J.E. Hundley ◽  
J.J. Windle ◽  
O. Alcantara ◽  
R. Linn ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Gene Promoter ◽  
Tartrate Resistant Acid Phosphatase ◽  
Trap Gene

Development and Characterization of Novel Monoclonal Antibodies Against Tartrate-Resistant Acid Phosphatase 5

Hybridoma ◽  
2006 ◽  
Vol 25 (6) ◽  
pp. 358-366 ◽  
Author(s):  
Tatsuya Ohashi ◽  
Toshihide Miura ◽  
Yoshihiko Igarashi ◽  
Iwao Kiyokawa ◽  
Yasuhito Sato ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Acid Phosphatase ◽  
Tartrate Resistant Acid Phosphatase

Tartrate-resistant acid phosphatase in serum of cancer patients.

1984 ◽  
Vol 30 (3) ◽  
pp. 457-459 ◽  
Author(s):  
K W Lam ◽  
C Dannaher ◽  
S Letchford ◽  
T Eastlund ◽  
C Y Li ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Enzyme Immunoassay ◽  
Cancer Patients ◽  
Acid Phosphatase Activity ◽  
Blood Donors ◽  
Colorimetric Method ◽  
Normal Blood ◽  
Tartrate Resistant Acid Phosphatase ◽  
Range Of Values

Abstract Tartrate-resistant acid phosphatase activity determined by enzyme immunoassay was higher in the serum of cancer patients than that in normal blood donors. The highest activity was found among patients having malignancy metastatic to bone. The classic colorimetric method showed a broad range of values among normal blood donors, and the contrast between normal and cancer patients was less obvious. Most of the cancer patients had normal to low alkaline phosphatase activities.

Generation and characterization of monoclonal antibodies to human type-5 tartrate-resistant acid phosphatase: development of a specific immunoassay of the isoenzyme in serum

1995 ◽  
Vol 41 (10) ◽  
pp. 1495-1499 ◽  
Author(s):  
P Chamberlain ◽  
J Compston ◽  
T M Cox ◽  
A R Hayman ◽  
R C Imrie ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Acid Phosphatase ◽  
Premenopausal Women ◽  
Tartrate Resistant Acid Phosphatase ◽  
Time Resolved ◽  
Specific Serum ◽  
Serum Trap ◽  
Human Osteoclast ◽  
The Mean

Abstract We have characterized four monoclonal antibodies (mAbs) to the purple ("tartrate-resistant," band 5) acid phosphatase of the human osteoclast (TRAP) and used these to develop a specific serum immunoassay. All four mAbs are of high affinity (Ka = 1-5 x 10(8) L/mol) with a very fast Kassoc (0.2-2.0 x 10(5) L mol-1 s-1) and a moderate Kdissoc (1-3 x 10(-3) s). Two of the mAbs were selected to develop a time-resolved fluorescence immunoassay to measure serum concentrations of TRAP. The mean serum immunoreactive TRAP in a group of healthy premenopausal women and men was 3.7 +/- 1.8 micrograms/L (mean +/- SD) and 3.5 +/- 1.6 micrograms/L, respectively. Significantly higher concentrations of TRAP were found in postmenopausal women (6.3 +/- 2.3 micrograms/L) and in eight patients with Gaucher disease (19.3 +/- 4.7 micrograms/L). Further studies are required to investigate the value of serum TRAP as a marker of bone resorption.

Relationship of plasma tartrate resistant acid phosphatase to the bone isoenzyme of serum alkaline phosphatase in hyperparathyroidism

1983 ◽  
Vol 133 (2) ◽  
pp. 189-200 ◽  
Author(s):  
J.J. Štěpán ◽  
E. Šilinková-Málková ◽  
T. Havránek ◽  
J. Formánková ◽  
M. Zichová ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Serum Alkaline Phosphatase ◽  
Tartrate Resistant Acid Phosphatase ◽  
Relationship Of
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