Hydrophobic properties of alkaline phosphatases.

The International journal of biochemistry (1986-01-01)
R W Wulkan, M I Huijskes-Heins, B Leijnse
ABSTRACT

The butanol extraction method of Morton (1950), a routine step in enzyme purification, is discussed with special reference to a hydrophobic form of alkaline phosphatase from human liver tissue. This form slowly precipitates from butanol-extracted liver tissue homogenates stored at 4 degrees C. Furthermore, it is lost when acetone precipitation is applied as a purification procedure. The soluble form in liver tissue is shown to have a higher relative hydrophobicity than the serum liver/bone isoenzyme. The use of sodium cholate in the isolation of the hydrophobic form produces an artefact in isoelectric focusing, which can be abolished by dialysis prior to focusing.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
1-Butanol, anhydrous, 99.8%
Sigma-Aldrich
1-Butanol, 99.9%
Sigma-Aldrich
1-Butanol, ACS reagent, ≥99.4%
Sigma-Aldrich
1-Butanol, for molecular biology, ≥99%
Sigma-Aldrich
1-Butanol, suitable for HPLC, ≥99.7%
Sigma-Aldrich
Butyl alcohol, natural, ≥99.5%, FCC, FG
Supelco
1-Butanol, analytical standard
Sigma-Aldrich
1-Butanol, puriss. p.a., ACS reagent, reag. ISO, reag. Ph. Eur., ≥99.5% (GC)
Sigma-Aldrich
1-Butanol, BioRenewable, ACS reagent, ≥99.4%
Supelco
1-Butanol, suitable for HPLC, 99.8%