| http://purl.uniprot.org/citations/1316152 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1316152 | http://www.w3.org/2000/01/rdf-schema#comment | "Nucleoside diphosphate (NDP) kinases have been found to be involved in a wide range of fundamental biological processes ranging from developmental control to signal transduction and metastasis. We have recently cloned and sequenced a cDNA encoding an NDP-kinase of the rat mucosal mast cell line RBL-2H3 [Hemmerich, S., Yarden, Y., & Pecht, I. (1992) Biochemistry (preceding paper in this issue)]. The enzyme itself has been isolated by means of its affinity to the bischromone cromoglycate. Here we report several of its biochemical characteristics: A structural model for the native protein is proposed in which two disulfide-linked pairs of similar 18-kDa subunits (p18) associate to form a 72-kDa tetramer (p72). This is based on the migration properties of the purified enzyme on gel filtration columns, sodium dodecylsulfate gel electrophoresis, and two-dimensional electrophoresis, together with peptide mapping data. In the absence of NDP, both intact p72 and the dissociated 18-kDa subunits (p18) were shown to undergo Mg(2+)-dependent stoichiometric autophosphorylation utilizing adenosine and guanosine triphosphate or gamma-thiotriphosphate as phosphate donor. This autophosphorylation activity was found to be retained by the 18-kDa subunits even following fractionation by SDS-PAGE and electrophoretic transfer to nitrocellulose. The Michaelis constant of this autophosphorylation reaction with either ATP, ATP gamma S, GTP, or GTP gamma S was determined to be 6.5 +/-1 microM, and maximally 2 mol of phosphate were found to be incorporated per p72 molecule, thus indicating that phosphorylation occurs at a single site on only two of the four 18-kDa subunits of the holoenzyme.(ABSTRACT TRUNCATED AT 250 WORDS)"xsd:string |
| http://purl.uniprot.org/citations/1316152 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi00134a007"xsd:string |
| http://purl.uniprot.org/citations/1316152 | http://purl.uniprot.org/core/author | "Pecht I."xsd:string |
| http://purl.uniprot.org/citations/1316152 | http://purl.uniprot.org/core/author | "Hemmerich S."xsd:string |
| http://purl.uniprot.org/citations/1316152 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1316152 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/1316152 | http://purl.uniprot.org/core/pages | "4580-4587"xsd:string |
| http://purl.uniprot.org/citations/1316152 | http://purl.uniprot.org/core/title | "Oligomeric structure and autophosphorylation of nucleoside diphosphate kinase from rat mucosal mast cells."xsd:string |
| http://purl.uniprot.org/citations/1316152 | http://purl.uniprot.org/core/volume | "31"xsd:string |
| http://purl.uniprot.org/citations/1316152 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/1316152 |
| http://purl.uniprot.org/citations/1316152 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/1316152 |
| http://purl.uniprot.org/uniprot/P19804#attribution-9A69E10F62B72F3A5328BF6F5C478839 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/1316152 |
| http://purl.uniprot.org/uniprot/#_P19804-mappedCitation-1316152 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/1316152 |
| http://purl.uniprot.org/uniprot/P19804 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/1316152 |