| pubmed-article:8615841 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8615841 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:8615841 | lifeskim:mentions | umls-concept:C0027950 | lld:lifeskim |
| pubmed-article:8615841 | lifeskim:mentions | umls-concept:C1546745 | lld:lifeskim |
| pubmed-article:8615841 | lifeskim:mentions | umls-concept:C0205148 | lld:lifeskim |
| pubmed-article:8615841 | lifeskim:mentions | umls-concept:C2251415 | lld:lifeskim |
| pubmed-article:8615841 | lifeskim:mentions | umls-concept:C1550658 | lld:lifeskim |
| pubmed-article:8615841 | pubmed:dateCreated | 1996-6-6 | lld:pubmed |
| pubmed-article:8615841 | pubmed:abstractText | An Arg-specific mono(ADP-ribosyl)transferase activity on the surface of human polymorphonuclear neutrophil leucocytes (PMNs) was confirmed by the use of diethylamino-(benzylidineamino)guanidine (DEA-BAG) as an ADP-ribose acceptor. Two separate HPLC systems were used to separate ADP-ribosyl-DEA-BAG from reaction mixtures, and its presence was confirmed by electrospray mass spectrometry. ADP-ribosyl-DEA-BAG was produced in the presence of PMNs, but not in their absence. Incubation of DEA-BAG with ADP-ribose (0.1-10 mM) did not yield ADP-ribosyl-DEA-BAG, which indicates that ADP-ribosyl-DEA-BAG formed in the presence of PMNs was not simply a product of a reaction between DEA-BAG and free ADP-ribose, due possibly to the hydrolysis of NAD+ by an NAD+ glycohydrolase. The assay of mono(ADP-ribosyl)transferase with agmatine as a substrate was modified for intact PMNs, and the activity was found to be approx. 50-fold lower than that in rabbit cardiac membranes. The Km of the enzyme for NAD+ was 100.1 30.4 microM and the Vmax 1.4 0.2 pmol of ADP-ribosylagmatine/h per 10(6) cells. The enzyme is likely to be linked to the cell surface via a glycosylphosphatidylinositol anchor, since incubation of intact PMNs with phosphoinositol-specific phospholipase C (PI-PLC) led to a 98% decrease in mono(ADP-ribosyl)transferase activity in the cells. Cell surface proteins were labelled after exposure of intact PMNs to [32P]NAD+. Their molecular masses were 79, 67, 46, 36 and 26 kDa. The time course for labelling was non-linear under these conditions over a period of 4 h. The labelled products were identified as mono(ADP-ribosyl)ated proteins by hydrolysis with snake venom phosphodiesterase to yield 5'-AMP. | lld:pubmed |
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| pubmed-article:8615841 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8615841 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8615841 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8615841 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8615841 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8615841 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:8615841 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:8615841 | pubmed:author | pubmed-author:MurraySS | lld:pubmed |
| pubmed-article:8615841 | pubmed:author | pubmed-author:TaylorG WGW | lld:pubmed |
| pubmed-article:8615841 | pubmed:author | pubmed-author:MacDermotJJ | lld:pubmed |
| pubmed-article:8615841 | pubmed:author | pubmed-author:LuMM | lld:pubmed |
| pubmed-article:8615841 | pubmed:author | pubmed-author:DonnellyL ELE | lld:pubmed |
| pubmed-article:8615841 | pubmed:author | pubmed-author:RendellN BNB | lld:pubmed |
| pubmed-article:8615841 | pubmed:author | pubmed-author:KefalasPP | lld:pubmed |
| pubmed-article:8615841 | pubmed:author | pubmed-author:AllportJ RJR | lld:pubmed |
| pubmed-article:8615841 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8615841 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8615841 | pubmed:volume | 315 ( Pt 2) | lld:pubmed |
| pubmed-article:8615841 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8615841 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8615841 | pubmed:pagination | 635-41 | lld:pubmed |
| pubmed-article:8615841 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:8615841 | pubmed:meshHeading | pubmed-meshheading:8615841-... | lld:pubmed |
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| pubmed-article:8615841 | pubmed:meshHeading | pubmed-meshheading:8615841-... | lld:pubmed |
| pubmed-article:8615841 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8615841 | pubmed:articleTitle | Arginine-specific mono(ADP-ribosyl)transferase activity on the surface of human polymorphonuclear neutrophil leucocytes. | lld:pubmed |
| pubmed-article:8615841 | pubmed:affiliation | Department of Clinical Pharmacology, Royal Postgraduate Medical School, London, U.K. | lld:pubmed |
| pubmed-article:8615841 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8615841 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:8615841 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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