-transparent.png){kind=logo}
The tartrate-resistant acid phosphatase was isolated from the spleen of a patient with leukemic reticuloendotheliosis. The unique characteristic of the enzyme is its similar reactivity toward p-nitrophenylphosphate, inorganic pyrophosphate ADP, and ATP. When ATP was incubated with the enzyme, the initial products were ADP and inorganic phosphate. The kinetic data confirmed that these substrates were hydrolyzed by the same enzyme. This type of substrate specificity is clearly different from acid phosphatase and pyrophosphatases previously described in the literature.
Related Publications
K W Lam, and
L C Lai, and
P T Burkart, and
L T Yam
January 1977,
Clinical chemistry,
K W Lam, and
L C Lai, and
P T Burkart, and
L T Yam
February 1971,
The New England journal of medicine,
K W Lam, and
L C Lai, and
P T Burkart, and
L T Yam
August 1981,
Clinical biochemistry,
K W Lam, and
L C Lai, and
P T Burkart, and
L T Yam
June 1980,
The Journal of biological chemistry,
K W Lam, and
L C Lai, and
P T Burkart, and
L T Yam
August 1972,
Archives of internal medicine,
K W Lam, and
L C Lai, and
P T Burkart, and
L T Yam
December 1972,
The American journal of pathology,
K W Lam, and
L C Lai, and
P T Burkart, and
L T Yam
February 1981,
Cancer,
K W Lam, and
L C Lai, and
P T Burkart, and
L T Yam
December 2004,
Nihon rinsho. Japanese journal of clinical medicine,
K W Lam, and
L C Lai, and
P T Burkart, and
L T Yam
February 2004,
Nihon rinsho. Japanese journal of clinical medicine,
K W Lam, and
L C Lai, and
P T Burkart, and
L T Yam
January 1985,
Enzyme,
