Substrate stabilization of lysophosphatidylcholine‐solubilized plasma membrane H+‐ATPase from oat roots
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Substrate stabilization of lysophosphatidylcholine‐solubilized plasma membrane H+‐ATPase from oat roots. / Palmgren, Michael Gjedde; Sommarin, Marianne; Jørgensen, Peter Leth.
In: Physiologia Plantarum, Vol. 74, No. 1, 09.1988, p. 20-25.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Substrate stabilization of lysophosphatidylcholine‐solubilized plasma membrane H+‐ATPase from oat roots
AU - Palmgren, Michael Gjedde
AU - Sommarin, Marianne
AU - Jørgensen, Peter Leth
PY - 1988/9
Y1 - 1988/9
N2 - Plasma membrane vesicles with H+‐ATPase activity were purified from 8‐day‐old oat (Avena sativa L. cv. Brighton) roots using an aqueous polymer two‐phase system. Of several detergents tested, only lysophosphatidylcholine solubilized the H+‐ATPase in an active form. Solubilization of the H+‐ATPase with lysophosphatidylcholine was possible in the absence of glycerol, but the ATPase activity decreased about 4–5 times as rapidly in the absence as in the presence of 30% (w/v) glycerol. The solubilized enzyme was further stabilized by ATP and protons. Addition of 1 mM ATP to the plasma membranes halted inactivation of the H+‐ATPase. Even in the absence of polyol compounds and ATP, the enzyme was stable for hours at relatively low pH with an optimum around pH 6.7 at room temperature. The curve for the stability of soluble H+‐ATPase as a function of pH closely resembles the pH curve for the activity of the H+‐ATPase. This suggests that binding of protons to transport sites may stabilize the soluble H+‐ATPase in an enzymatically active form.
AB - Plasma membrane vesicles with H+‐ATPase activity were purified from 8‐day‐old oat (Avena sativa L. cv. Brighton) roots using an aqueous polymer two‐phase system. Of several detergents tested, only lysophosphatidylcholine solubilized the H+‐ATPase in an active form. Solubilization of the H+‐ATPase with lysophosphatidylcholine was possible in the absence of glycerol, but the ATPase activity decreased about 4–5 times as rapidly in the absence as in the presence of 30% (w/v) glycerol. The solubilized enzyme was further stabilized by ATP and protons. Addition of 1 mM ATP to the plasma membranes halted inactivation of the H+‐ATPase. Even in the absence of polyol compounds and ATP, the enzyme was stable for hours at relatively low pH with an optimum around pH 6.7 at room temperature. The curve for the stability of soluble H+‐ATPase as a function of pH closely resembles the pH curve for the activity of the H+‐ATPase. This suggests that binding of protons to transport sites may stabilize the soluble H+‐ATPase in an enzymatically active form.
KW - Avena sativa
KW - H‐ATPase
KW - lysophosphatidylcholine
KW - oat
KW - plasma membrane
KW - two‐phase partitioning
UR - http://www.scopus.com/inward/record.url?scp=84989758907&partnerID=8YFLogxK
U2 - 10.1111/j.1399-3054.1988.tb04935.x
DO - 10.1111/j.1399-3054.1988.tb04935.x
M3 - Journal article
AN - SCOPUS:84989758907
VL - 74
SP - 20
EP - 25
JO - Physiologia Plantarum
JF - Physiologia Plantarum
SN - 0031-9317
IS - 1
ER -
ID: 245001861