| pubmed-article:7569316 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7569316 | lifeskim:mentions | umls-concept:C0205101 | lld:lifeskim |
| pubmed-article:7569316 | lifeskim:mentions | umls-concept:C0053409 | lld:lifeskim |
| pubmed-article:7569316 | lifeskim:mentions | umls-concept:C0425245 | lld:lifeskim |
| pubmed-article:7569316 | lifeskim:mentions | umls-concept:C1996904 | lld:lifeskim |
| pubmed-article:7569316 | lifeskim:mentions | umls-concept:C1880497 | lld:lifeskim |
| pubmed-article:7569316 | lifeskim:mentions | umls-concept:C2700289 | lld:lifeskim |
| pubmed-article:7569316 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:7569316 | pubmed:dateCreated | 1995-11-2 | lld:pubmed |
| pubmed-article:7569316 | pubmed:abstractText | Electrophoretic mobility of secreted invertase (E.C. 3.2.1.26) from gelatin-immobilized yeast cells was analysed and compared with that of secreted invertase from freely suspended batch-grown cells. Invertase from immobilized cells showed a lower mobility after 24 h of incubation, in medium containing either glucose or raffinose as carbon source. Changes in invertase mobility were also followed in a time course both for immobilized and for freely suspended batch-grown cells. Mobility of invertase from free cells increased after approximately 15 h of incubation, independently of the carbon source, whilst that of invertase from immobilized cells remained constant. The differences observed were attributed to a different level of glycosylation of the protein moiety in free and immobilized cells. The amount of mannoproteins in the cell walls of immobilized cells was also investigated by ConA-ferritin labelling and quantification of ferritin particle density in ultrathin sections; the results of this experiment showed a higher content of mannoproteins in the walls of immobilized cells when compared with free cells. As a whole, these results are indicative of physiological changes that can be ascribed to the peculiar microenvironment of gel-immobilized cells. | lld:pubmed |
| pubmed-article:7569316 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7569316 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7569316 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7569316 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7569316 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7569316 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7569316 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7569316 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7569316 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7569316 | pubmed:issn | 0923-2508 | lld:pubmed |
| pubmed-article:7569316 | pubmed:author | pubmed-author:SentandreuRR | lld:pubmed |
| pubmed-article:7569316 | pubmed:author | pubmed-author:RicoHH | lld:pubmed |
| pubmed-article:7569316 | pubmed:author | pubmed-author:de AlteriisEE | lld:pubmed |
| pubmed-article:7569316 | pubmed:author | pubmed-author:ParascandolaP... | lld:pubmed |
| pubmed-article:7569316 | pubmed:author | pubmed-author:ZuechSS | lld:pubmed |
| pubmed-article:7569316 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7569316 | pubmed:volume | 146 | lld:pubmed |
| pubmed-article:7569316 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7569316 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7569316 | pubmed:pagination | 217-25 | lld:pubmed |
| pubmed-article:7569316 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:7569316 | pubmed:meshHeading | pubmed-meshheading:7569316-... | lld:pubmed |
| pubmed-article:7569316 | pubmed:meshHeading | pubmed-meshheading:7569316-... | lld:pubmed |
| pubmed-article:7569316 | pubmed:meshHeading | pubmed-meshheading:7569316-... | lld:pubmed |
| pubmed-article:7569316 | pubmed:meshHeading | pubmed-meshheading:7569316-... | lld:pubmed |
| pubmed-article:7569316 | pubmed:meshHeading | pubmed-meshheading:7569316-... | lld:pubmed |
| pubmed-article:7569316 | pubmed:meshHeading | pubmed-meshheading:7569316-... | lld:pubmed |
| pubmed-article:7569316 | pubmed:meshHeading | pubmed-meshheading:7569316-... | lld:pubmed |
| pubmed-article:7569316 | pubmed:meshHeading | pubmed-meshheading:7569316-... | lld:pubmed |
| pubmed-article:7569316 | pubmed:articleTitle | Electrophoretic mobility of external invertase from free and gel-immobilized yeast cells. | lld:pubmed |
| pubmed-article:7569316 | pubmed:affiliation | Dip. to Fisiologia Generale, Università degli Studi di Napoli, Italy. | lld:pubmed |
| pubmed-article:7569316 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7569316 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:7569316 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
