Showing papers on "Tartrate-resistant acid phosphatase published in 1977"
TL;DR: 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, which has properties different from the pyrophosphatase previously observed in normal animal tissues.
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.
39 citations
TL;DR: Prolymphocytic leukaemia (PL) is a rare variant of CLL, clearly defined by Galton et al.
Abstract: Prolymphocytic leukaemia (PL) is a rare variant of CLL, clearly defined by Galton et al. [8]. Among 10 patients with PL 9 patients had B-cell characteristics, only 1 patient was described to have T-lymphocyte markers [2].
20 citations
TL;DR: The tartrate-resistant acid phosphatase was isolated from the spleen of a patient with leukemic reticuloendotheliosis and its unique characteristic is its similar reactivity toward p-nitrophenylphosphate, inorganic pyrophosphate ADP, and ATP.
9 citations