| RRC ID |
77237
|
| Author |
Wang L, Shimizu Y, Mizunaga T, Matsumoto S, Otsuka Y.
|
| Title |
Expression, purification and characterization of yeast protein disulfide isomerase produced by a recombinant baculovirus-mediated silkworm, Bombyx mori, pupae expression system.
|
| Journal |
Biotechnol Lett
|
| Abstract |
Protein disulfide isomerase (PDI) is a multifunctional polypeptide presents in the endoplasmic reticulum of the cell. Silkworm (Bombyx mori) pupae were used as hosts to produce recombinant PDI (rPDI). The concentration-dependent chaperone activity of rPDI was evidenced by the inhibition of the aggregation of rhodanese. Approximately 297 microg rPDI was purified from a single silkworm pupa. Results of rPDI treated with endoglycosidase H and N-glycanase, PNGase F, indicate that non-N-glycosylated rPDI (occupying 90%) and N-glycosylated rPDI are expressed in the silkworm expression system. The difference in glycosylation between silkworm pupae and yeast is discussed.
|
| Volume |
30(4)
|
| Pages |
625-30
|
| Published |
2008-4-1
|
| DOI |
10.1007/s10529-007-9582-4
|
| PMID |
17985081
|
| MeSH |
Animals
Baculoviridae / genetics*
Blotting, Western
Bombyx / genetics*
Electrophoresis, Polyacrylamide Gel
Fungal Proteins / genetics
Fungal Proteins / isolation & purification
Fungal Proteins / metabolism*
Glycosylation
Protein Disulfide-Isomerases / genetics
Protein Disulfide-Isomerases / isolation & purification
Protein Disulfide-Isomerases / metabolism*
Pupa / genetics
Recombinant Proteins / isolation & purification
Recombinant Proteins / metabolism
Yeasts / enzymology*
Yeasts / genetics
|
| IF |
1.977
|
| Resource |
| Human and Animal Cells |
BmN |
