The use of multifunctional adsorbents to purify membrane-bound phosphatases from Zymomonas mobilis. Purification of acid phosphatase, alkaline phosphatase and ATPase.
The purification of detergent-solubilized membrane-bound phosphatases from Zymomonas mobilis using novel adsorbents is described. The prepared adsorbents have a hydrophobic core with functional groups attached. These functional groups may either increase or decrease the hydrophobicity of the adsorbent, or participate in other forms of interactions. Adsorption of acid phosphatase (ACP), alkaline phosphatase (ALP) and ATPase to these adsorbents was salt-promoted. Desorption was achieved by decreasing the salt concentration or by displacement with increasing concentration of Triton X-100. The results indicate that chromatography on multifunctional adsorbents that are predominantly hydrophobic in character is a procedure that can have a general applicability in purification of membrane proteins.
Reyes
L B
LB
Department of Biochemistry, La Trobe University, Bundoora, Victoria, Australia.
Scopes
R K
RK
D000135:Acid Phosphatase / Q000302:isolation & purification*; D000251:Adenosine Triphosphatases / Q000302:isolation & purification*; D000469:Alkaline Phosphatase / Q000302:isolation & purification*; D006090:Gram-Negative Bacteria / Q000201:enzymology*; D008565:Membrane Proteins / Q000302:isolation & purification*
D008565:Membrane Proteins; D000469:Alkaline Phosphatase; D000135:Acid Phosphatase; D000251:Adenosine Triphosphatases