Abstract
Precipitation agents were developed to perform protein separation by precipitation based on hydrophobic interaction. They consisted of ligands, saturated linear chains of fatty acids, attached by esterification to a carrier molecule, methylcellulose. Precipitation of bovine serum albumin was achieved at 50 percent saturation of ammonium sulfate. The butyric acid derivative showed a higher efficiency in precipitating this protein than other derivatives tested. There is evidence that the interaction between the protein and the derivatives is hydrophobic.
| Language | English (US) |
|---|---|
| Pages | 1-12 |
| Number of pages | 12 |
| Journal | Brazilian Journal of Chemical Engineering |
| Volume | 12 |
| Issue number | 1 |
| State | Published - 1995 |
Profile
ASJC Scopus subject areas
- Chemical Engineering(all)
Cite this
Development of precipitant agents for precipitation of proteins based on hydrophobic interaction. / Miranda, E. A.; Berglund, K. A.
In: Brazilian Journal of Chemical Engineering, Vol. 12, No. 1, 1995, p. 1-12.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Development of precipitant agents for precipitation of proteins based on hydrophobic interaction
AU - Miranda,E. A.
AU - Berglund,K. A.
PY - 1995
Y1 - 1995
N2 - Precipitation agents were developed to perform protein separation by precipitation based on hydrophobic interaction. They consisted of ligands, saturated linear chains of fatty acids, attached by esterification to a carrier molecule, methylcellulose. Precipitation of bovine serum albumin was achieved at 50 percent saturation of ammonium sulfate. The butyric acid derivative showed a higher efficiency in precipitating this protein than other derivatives tested. There is evidence that the interaction between the protein and the derivatives is hydrophobic.
AB - Precipitation agents were developed to perform protein separation by precipitation based on hydrophobic interaction. They consisted of ligands, saturated linear chains of fatty acids, attached by esterification to a carrier molecule, methylcellulose. Precipitation of bovine serum albumin was achieved at 50 percent saturation of ammonium sulfate. The butyric acid derivative showed a higher efficiency in precipitating this protein than other derivatives tested. There is evidence that the interaction between the protein and the derivatives is hydrophobic.
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UR - http://www.scopus.com/inward/citedby.url?scp=0029493526&partnerID=8YFLogxK
M3 - Article
VL - 12
SP - 1
EP - 12
JO - Brazilian Journal of Chemical Engineering
T2 - Brazilian Journal of Chemical Engineering
JF - Brazilian Journal of Chemical Engineering
SN - 0104-6632
IS - 1
ER -