Co-purification of Glucanase with Acid Trehalase–Invertase Aggregate in Saccharomyces Cerevisiae
IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata
View Archive Info| Field | Value | |
| Title |
Co-purification of Glucanase with Acid Trehalase–Invertase
Aggregate in Saccharomyces Cerevisiae
|
|
| Creator |
Basu, Arghya
Chaudhuri , Paramita Malakar , Dipankar Ghosh, Anil K |
|
| Subject |
Drug Development/Diagnostics & Biotechnology
|
|
| Description |
An electrophoretically homogenous
aggregate of acid trehalase, invertase and an unidentified
37–41 kDa protein was purified from
Saccharomyces cerevisiae. N-terminal analysis of
the protein revealed an amino acid sequence identical
to that of Bgl2p (endo-b-l,3-glucanase) of S. cerevisiae.
Acid trehalase activity with co-eluted glucanase
activity was observed from late growth phase through
early stationary phase. Pools with high percentage of
Bgl2p corresponded with high acid trehalase activity.
A BGL2 deletion strain had lower acid trehalase
activity. The 37–41 kDa protein represents Bgl2p
which, besides imparting glucanase activity, could
also be acting as a regulator for the acid trehalase
activity by association in the enzyme aggregate.
|
|
| Publisher |
Kluwer
|
|
| Date |
2008
|
|
| Type |
Article
PeerReviewed |
|
| Format |
application/pdf
|
|
| Identifier |
http://www.eprints.iicb.res.in/297/1/BIOTECHNOLOGY_LETTERS%2C30(_2)%2C___299%2D304%2C2008[128].pdf
Basu, Arghya and Chaudhuri , Paramita and Malakar , Dipankar and Ghosh, Anil K (2008) Co-purification of Glucanase with Acid Trehalase–Invertase Aggregate in Saccharomyces Cerevisiae. Biotechnology Letters, 30 (2). pp. 299-304. |
|
| Relation |
http://dx.doi.org/10.1007/s10529-007-9535-y
http://www.eprints.iicb.res.in/297/ |
|