Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1989-12-4
|
| pubmed:abstractText |
Growth of Saccharomyces cerevisiae cells in a synthetic buffered culture medium resulted in the secretion of high levels of two soluble exoglucanases which were purified by a procedure involving one (exglucanase II) and two (exoglucanase I) steps, respectively. Once treated with endoglucosaminidase H (Endo H) both enzymes behaved indistinguishably when analyzed by SDS-PAGE, high pressure liquid chromatography (HPLC) and ionic exchange chromatography. Exoglucanase I, the isoenzyme with higher carbohydrate content, exhibited a higher Km against laminarin and a higher thermal stability than exoglucanase II. However, once the enzymes were deglycosylated in vitro these parameters turned out to be identical. These results suggest that both exoglucanases share a very similar, if not identical protein portion and accordingly may be product of either the same gene or a family of related genes.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Oct
|
| pubmed:issn |
0213-4101
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
3
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
195-203
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading | |
| pubmed:year |
1987
|
| pubmed:articleTitle |
Purification of two exoglucanases secreted by Saccharomyces cerevisiae and partial characterization of their protein moieties.
|
| pubmed:affiliation |
Departamento de Microbiología, Facultad de Ciencias, Universidad de Extremadura, Badajoz, Spain.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|