PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 13027

Terminal deoxynucleotidyl transferase as a biological marker for human leukemia.

P S Sarin·R C Gallo
View original source ↗Export metadata ↓

Abstract

High levels of terminal deoxynucleotidyl transferase have been observed in leukocytes of 7 out of 20 patients with chronic myelogenous leukemia in acute blast phase of the disease. These levels are comparable to the levels observed in human and calf thymus gland and cell lines with some T cell characteristics (Molt 4 and 8402). Negligible levels of this activity were observed in chronic myelogenous leukemia not in an acute blast phase of the disease, chronic lymphocytic leukemia, human B cells, mature T cells, and the mixed population of lymphocytes present in normal human blood. The detection of this enzyme in some patients with chronic myelogenous leukemia in acute blast phase of the disease suggests that the blast proliferation may involve primitive stem cells which have more lymphoid than myelogenous characteristics. This enzyme assay may be of use as a biological marker for following patients during treatment and in remission.

Explore related subjects

Cations, DivalentCell LineDeoxyribonucleotidesDiphosphatesEthylmaleimideHumansHydrogen-Ion ConcentrationLeukemia, LymphoidLeukemia, MyeloidLeukemia, Myeloid, AcuteLeukocytesLymphocytesNucleotidyltransferasesOligonucleotidesJournal Article

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

P S Sarin, R C Gallo. 1976. Terminal deoxynucleotidyl transferase as a biological marker for human leukemia.. https://doi.org/10.1007/978-3-642-87524-3_47

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed1979

5'-Hydroxyl polyribonucleotide kinase from HeLa cell nuclei. Purification and properties.

An enzyme, 5'-hydroxyl polyribonucleotide kinase, which catalyzes the phosphorylation of 5'-hydroxyl ends of RNA in the presence of ATP, has been isolated from extracts of HeLa cell nuclei. The kinase requires a divalent cation (Mg2+ or Mn2+) for activity, has an alkaline pH optimum, and is sensitive to the sulfhydryl antagonist N-ethylmaleimide. 5'-hydroxyl terminated polydeoxyribonucleotides are phosphorylated much less efficiently than the 5'-hydroxyl terminated polyribonucleotides, and the kinase preparation is inactive on ribonucleoside 3'-monophosphates. Enzyme activity is inhibited by ADP and by pyrophosphate. The sedimentation coefficient of the kinase is estimated to be 5.6 S from glycerol gradient centrifugation.

Cations, Divalent↗
PubMed1979

PaeExo IX: a unique deoxyribonuclease from Pseudomonas aeruginosa active in the presence of EDTA.

A new deoxyribonuclease, PaeExo IX, has been purified to electrophoretic homogeneity from extracts of Pseudomonas aeruginosa strain PAO. This enzyme, which is active in the presence of EDTA, is equally efficient in hydrolyzing native and heart-denatured DNA to acid-s-luble products. The enzyme is partially or totally inhibited by the presence of several divalent cations. The active protein has a molecular weight of 1.6 +/- 0.1 x 10(5) and is composed of two nonidentical polypeptides with molecular weights of 78,000 and 69,000.

Cations, Divalent↗
PubMed1979

The formation of enzyme-bound and medium pyrophosphate and the molecular basis of the oxygen exchange reaction of yeast inorganic pyrophosphatase.

Yeast inorganic pyrophosphatase, with 10 mM 32Pi and 10 mM Mg2+ present at pH 7.3 TO 7.6, rapidly forms enzyme-bound pyrophosphate equivalent to about 5% of the total catalytic sties on the two enzyme subunits. The enzyme thus appears to bind PPi so as to favor thermodynamically its formation from Pi. The enzyme catalyzes a measurable equilibrium formation of free PPi at a much slower rate. Under similar conditions, the enzyme catalyzes a rapid exchange of oxygen atoms between Pi and water with the relative activation by metals being Mg2+ greater than Zn2+ greater than Co2+ greater than Mn2+. Millisecond mixing and quenching experiments demonstrate that the rate of formation and cleavage of the enzyme-bound PPi is rapid enough to explain most or all of the oxygen exchange reaction.

Cations, Divalent↗