Purification and some properties of sodom-apple latex proteinases
β Scribed by O.C. Aworh; V. Kasche; O.O. Apampa
- Publisher
- Elsevier Science
- Year
- 1994
- Tongue
- English
- Weight
- 1008 KB
- Volume
- 50
- Category
- Article
- ISSN
- 0308-8146
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Pectinesterase from apple was separated into two fractions by chromatography on Sephadex G-75. The major pectinesterase was purified by cationexchange chromatography on CM-Sephadex C-50. It had a molecular mass of 36 kDa, and isoelectric point of about 9, similar to one of the major pectinesterases
## Abstract A cysteine proteinase from sorghum malt variety SK5912 was purified by a combination of 4 M sucrose fractionation, ionβexchange chromatography on Qβ and SβSepharose (fast flow), gel filtration chromatography on Sephadex Gβ100 and hydrophobic interaction chromatography on Phenyl Sepharos