| pubmed-article:8240242 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8240242 | lifeskim:mentions | umls-concept:C0017786 | lld:lifeskim |
| pubmed-article:8240242 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:8240242 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:8240242 | pubmed:dateCreated | 1993-12-3 | lld:pubmed |
| pubmed-article:8240242 | pubmed:abstractText | We previously identified a 50 kDa membrane protein which bound to in vitro assembled microtubules [Mithieux and Rousset (1989) J. Biol. Chem. 264, 4664-4668]. This protein exhibited the expected properties for mediating the ATP-dependent association of vesicles with microtubules [Mithieux, Audebet and Rousset (1988) Biochim. Biophys. Acta 969, 121-130]. The 50 kDa membrane protein (MP50), initially extracted in very low amount from isolated pig thyroid lysosomes/endosomes, has now been purified from membrane preparations of crude vesicle fractions from pig liver and brain. MP50 was isolated from detergent-solubilized membrane protein by affinity chromatography on immobilized ATP; 3-5 mg of MP50 was obtained from 100 g of liver tissue. Phase partitioning in Triton X-114 indicated that MP50 is a peripheral membrane protein. Radioiodinated liver MP50 bound to microtubules assembled in vitro. The binding was inhibited by ATP (Ki = 0.76 mM) and displaced by unlabelled liver or brain MP50. Equilibrium binding studies yielded KD values of 1.8 x 10(-7) M. By N-terminal amino acid sequence analysis, MP50 was identified as glutamate dehydrogenase (GDH), by comparison of V8 protease peptide maps of MP50 with purified liver GDH. Liver MP50 exhibited a low GDH activity; 4-5 units/mg compared with 18 and 34 units/mg for purified bovine and rat liver GDH respectively. Bovine and rat liver GDH yielded six spots from pI 5.7 to 7.2 when analysed by two-dimensional electrophoresis; in contrast, MP50 gave one main spot (corresponding to spot 2 of liver GDH) with a pI of approx. 6.5. Soluble liver GDH from commercial sources exhibited a very low or no microtubule-binding activity. In conclusion, we have found a membrane-bound form of GDH capable of specific and nucleotide-sensitive interaction with microtubules. Our data suggest that GDH isoproteins, the number of which has been undervalued up to now, could have cellular functions other than that of an enzyme. | lld:pubmed |
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| pubmed-article:8240242 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8240242 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8240242 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8240242 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8240242 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:8240242 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:8240242 | pubmed:author | pubmed-author:RoussetBB | lld:pubmed |
| pubmed-article:8240242 | pubmed:author | pubmed-author:RajaiHH | lld:pubmed |
| pubmed-article:8240242 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8240242 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8240242 | pubmed:volume | 295 ( Pt 2) | lld:pubmed |
| pubmed-article:8240242 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8240242 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8240242 | pubmed:pagination | 447-55 | lld:pubmed |
| pubmed-article:8240242 | pubmed:dateRevised | 2010-9-13 | lld:pubmed |
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| pubmed-article:8240242 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8240242 | pubmed:articleTitle | A membrane-bound form of glutamate dehydrogenase possesses an ATP-dependent high-affinity microtubule-binding activity. | lld:pubmed |
| pubmed-article:8240242 | pubmed:affiliation | Institut National de la Santé et de la Recherche Médicale, Unité 369, Faculté de Médecine Alexis Carrel, Lyon, France. | lld:pubmed |
| pubmed-article:8240242 | pubmed:publicationType | Journal Article | lld:pubmed |
