Substrate stabilization of lysophosphatidylcholine‐solubilized plasma membrane H+‐ATPase from oat roots

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

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

Harvard

Palmgren, MG, Sommarin, M & Jørgensen, PL 1988, 'Substrate stabilization of lysophosphatidylcholine‐solubilized plasma membrane H+‐ATPase from oat roots', Physiologia Plantarum, vol. 74, no. 1, pp. 20-25. https://doi.org/10.1111/j.1399-3054.1988.tb04935.x

APA

Palmgren, M. G., Sommarin, M., & Jørgensen, P. L. (1988). Substrate stabilization of lysophosphatidylcholine‐solubilized plasma membrane H+‐ATPase from oat roots. Physiologia Plantarum, 74(1), 20-25. https://doi.org/10.1111/j.1399-3054.1988.tb04935.x

Vancouver

Palmgren MG, Sommarin M, Jørgensen PL. Substrate stabilization of lysophosphatidylcholine‐solubilized plasma membrane H+‐ATPase from oat roots. Physiologia Plantarum. 1988 Sep;74(1):20-25. https://doi.org/10.1111/j.1399-3054.1988.tb04935.x

Author

Palmgren, Michael Gjedde ; Sommarin, Marianne ; Jørgensen, Peter Leth. / Substrate stabilization of lysophosphatidylcholine‐solubilized plasma membrane H+‐ATPase from oat roots. In: Physiologia Plantarum. 1988 ; Vol. 74, No. 1. pp. 20-25.

Bibtex

@article{9eb651084f7f4a9d921e740a33c16fb4,
title = "Substrate stabilization of lysophosphatidylcholine‐solubilized plasma membrane H+‐ATPase from oat roots",
abstract = "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.",
keywords = "Avena sativa, H‐ATPase, lysophosphatidylcholine, oat, plasma membrane, two‐phase partitioning",
author = "Palmgren, {Michael Gjedde} and Marianne Sommarin and J{\o}rgensen, {Peter Leth}",
year = "1988",
month = sep,
doi = "10.1111/j.1399-3054.1988.tb04935.x",
language = "English",
volume = "74",
pages = "20--25",
journal = "Physiologia Plantarum",
issn = "0031-9317",
publisher = "Wiley-Blackwell",
number = "1",

}

RIS

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