Regulation of human lymphoblast plasma membrane 5'-nucleotidase by zinc.
نویسندگان
چکیده
منابع مشابه
Altered properties of human T-lymphoblast soluble low Km 5'-nucleotidase: comparison with B-lymphoblast enzyme.
Soluble low Km 5'-nucleotidases have been purified from human cultured T- and B-lymphoblasts to compare their properties and to examine the mechanism of different rates of nucleotide dephosphorylation. The enzyme from B-lymphoblasts (MGL-8) was 4385-fold purified with a specific activity of 114 mumol/min/mg, while the enzyme from T-lymphoblasts (CEM, MOLT-4) was 4355-fold purified with a specif...
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BACKGROUND/AIMS Modulation of extracellular adenine nucleotide and adenosine concentrations is one potential mechanism by which docosahexaenoic acid (DHA) may exert beneficial effects in critically ill patients. This study assessed DHA effects on extracellular adenine purines. METHODS Experiments used human pulmonary endothelial cells (HPMEC) and umbilical vein endothelial cells (HUVEC) treat...
متن کاملThe origin of biphasic Arrhenius plots of rat liver plasma-membrane 5'-nucleotidase [proceedings].
Intrinsic membrane proteins, which may only be solubilized by procedures that disrupt membrane structure, must all have domains that interact with their non-polar environment. The degree of interaction, however, varies from a strict requirement of phospholipid for activity (e.g. Ca2+-activated adenosine triphosphatase; Warren et al., 1974) t o a requirement for structural support only (e.g. cyt...
متن کاملThe properties and extracellular location of 5'-nucleotidase of the rat fat-cell plasma membrane.
1. A phosphohydrolase specific for 5'-nucleotides was characterized by using a particulate fraction from isolated fat-cells. 2. The activity of intact cells towards 5'-AMP was studied. 3. The activity in either situation had the same KM for AMP (45 muM) and was inhibited by low concentrations of ATP (less than 50 muM), but less potently by the ATP analogues AMP-P(CH2)P(adenylyl (beta gamma-meth...
متن کاملHigh Km soluble 5'-nucleotidase from human placenta. Properties and allosteric regulation by IMP and ATP.
A human placental soluble "high Km" 5'-nucleotidase has been separated from "low Km" 5'-nucleotidase and nonspecific phosphatase by AMP-Sepharose affinity chromatography. The enzyme was purified 8000-fold to a specific activity of 25.6 mumol/min/mg. The subunit molecular mass is 53 kDa, and the native molecular mass is 210 kDa, suggesting a tetrameric structure. Soluble high Km 5'-nucleotidase ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1982
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)33481-1