Comparative study of alkaline phosphatase activity in lymphocytes, mitogen-induced blasts, lymphoblastoid cell lines, acute myeloid leukemia, and chronic lymphatic leukemia cells (N-alkaline phosphatase/thiophosphoric acid thioesters)

Journal Article · Sat May 01 00:00:00 EDT 1976 · Proc. Natl. Acad. Sci. U.S.A.; (United States)

DOI:https://doi.org/10.1073/pnas.73.5.1432· OSTI ID:7116113

Neumann, H ^[1]; Klein, E; Hauck-Granoth, R; Yachnin, S; Ben-Bassat, H

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1. Weizmann Inst. of Science, Rehovoth, Israel

Alkaline phosphatase (orthophosphoricmonoester phosphohydrolase (alkaline pH optimum), EC 3.1.3.1) purified from a Burkitt lymphoma cell line (Daudi) and Moloney-virus-induced murine leukemia (YAC) showed unique catalytic properties in substrate specificity and inhibition by cysteamine-S-phosphate. It migrated on polyacrylamide gel electrophoresis in a single activity band. Alkaline phosphatase with similar properties was found in several human lymphoblastoid cell lines, in chronic lymphatic leukemic cells, in organs of leukemic mice, and in sera of patients with certain lymphoproliferative disorders. The unique kinetic properties of this enzyme were established using two kinds of substrate, namely, the monoesters of orthophosphoric acid (Type I) and the S-substituted monoesters of thiophosphoric acid (Type II). The enzyme catalyzed the hydrolysis of Type I, but failed to hydrolyze Type II. The enzyme probably interacts directly either in catalysis or in binding with the --P--O-- or --P--S-- bonds. Thus, in these respects it differs from the established enzymatic mechanism of other known alkaline phosphatases, and therefore can be considered a new enzyme. This enzyme was designated N-alkaline phosphatase. N-alkaline phosphatase was absent in untreated and mitogen-stimulated human blood lymphocytes, in murine lymph nodes, and pig thymus (even after mitogen stimulation), and in blast cells of acute myeloid leukemic patients. The appearance of N-alkaline phosphatase only in certain types of proliferating lymphocytes and in the sera of patients with lymphoproliferative disorders may be exploited as a cell marker and as a diagnostic tool.

• OSTI ID: 7116113
• Journal Information: Proc. Natl. Acad. Sci. U.S.A.; (United States), Vol. 73:5
• Country of Publication: United States
• Language: English

Related Subjects

62 RADIOLOGY AND NUCLEAR MEDICINE
59 BASIC BIOLOGICAL SCIENCES
ALKALINE PHOSPHATASE
CATALYSIS
LEUKEMIA
DIAGNOSIS
LYMPHOCYTES
ANIMAL CELLS
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
CONNECTIVE TISSUE CELLS
DISEASES
ENZYMES
ESTERASES
HEMIC DISEASES
HYDROLASES
LEUKOCYTES
NEOPLASMS
PHOSPHATASES
SOMATIC CELLS
550600* - Medicine
551000 - Physiological Systems