Performance of hydrophobic chromatography in purification of α-amylase
✍ Scribed by Eizo Sada; Shigeo Katoh; Tsuneo Inoue; Masami Shiozawa
- Publisher
- John Wiley and Sons
- Year
- 1985
- Tongue
- English
- Weight
- 405 KB
- Volume
- 27
- Category
- Article
- ISSN
- 0006-3592
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
A 4- to 6-kDa hydrophobic peptide (SP4-6) was purified from human pulmonary surfactant. Sep Pak Florisil cartridges removed most of the lipids and the 18-kDa peptide. Analytical wide-pore reversed-phase HPLC column separated a single peptide that contained no detectable lipids (less than 1 nmol/2.5
An affinity chromatography technique for purification of oc-amylase from triticale (X Triticosecale Wittmack) is described. Triticale ol-amylase is retained on a column of cyclohepta-amylose epoxy Sepharose 6B. Contaminating proteins pass through in the sodium acetate elution buffer whereas the cy-a
Soybean glycinin and KUNITZ trypsin inhibitor were purified by hydrophobic chromatography on Phenyl Sepharose which removes the admixtures of more hydrophobic proteins and of some non-protein UV-absorbing substances. ## Zusammenfassung Reinigung einiger Sojabohnenproteine durch hydrophobe Chromat
Purification and properties of a-amylase from Micrococcus variuns ADEYEMI I . ADELEYE i Rcc?ird I 0 .4u</i~s/ 19cYYiArccy,tetl 6 FdJruciry I9901 An extraccllular cx-amylase from Micrococcus ivxinns was partially purified (63 fold) by ammonium sulphate precipitation followed by dialysis and separate