Proteolytic activation of the plant plasma membrane H+-ATPase by removal of a terminal segment

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Standard

Proteolytic activation of the plant plasma membrane H+-ATPase by removal of a terminal segment. / Palmgren, M. G.; Larsson, C.; Sommarin, M.

In: Journal of Biological Chemistry, Vol. 265, No. 23, 1990, p. 13423-13426.

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

Harvard

Palmgren, MG, Larsson, C & Sommarin, M 1990, 'Proteolytic activation of the plant plasma membrane H+-ATPase by removal of a terminal segment', Journal of Biological Chemistry, vol. 265, no. 23, pp. 13423-13426.

APA

Palmgren, M. G., Larsson, C., & Sommarin, M. (1990). Proteolytic activation of the plant plasma membrane H+-ATPase by removal of a terminal segment. Journal of Biological Chemistry, 265(23), 13423-13426.

Vancouver

Palmgren MG, Larsson C, Sommarin M. Proteolytic activation of the plant plasma membrane H+-ATPase by removal of a terminal segment. Journal of Biological Chemistry. 1990;265(23):13423-13426.

Author

Palmgren, M. G. ; Larsson, C. ; Sommarin, M. / Proteolytic activation of the plant plasma membrane H+-ATPase by removal of a terminal segment. In: Journal of Biological Chemistry. 1990 ; Vol. 265, No. 23. pp. 13423-13426.

Bibtex

@article{46f7a39a27824e2bb950e59fb3d64a1f,
title = "Proteolytic activation of the plant plasma membrane H+-ATPase by removal of a terminal segment",
abstract = "Incubation of oat root plasma membrane vesicles in the presence of ATP with trypsin or chymotrypsin increased the rate of ATP hydrolysis and ATP-dependent proton pumping by the plasma membrane H+-ATPase. Proton pumping was stimulated more than 200%, whereas ATP hydrolytic activity was stimulated about 30%. The K(m)(ATP) for both proton pumping and ATP hydrolysis was lowered from about 0.3 mM to below 0.1 mM. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of trypsin-treated plasma membranes revealed a decrease in a 100-kDa band and the appearance of a 93-kDa band. Western blot analysis using antibodies against the H+-ATPase showed that both of these bands represented the H+-ATPase and suggested that a 7-kDa segment was released. Extensive treatment with cardoxypeptidase A also activated the H+-ATPase indicating that the 7-kDa segment originated from the C terminus.",
author = "Palmgren, {M. G.} and C. Larsson and M. Sommarin",
year = "1990",
language = "English",
volume = "265",
pages = "13423--13426",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "23",

}

RIS

TY - JOUR

T1 - Proteolytic activation of the plant plasma membrane H+-ATPase by removal of a terminal segment

AU - Palmgren, M. G.

AU - Larsson, C.

AU - Sommarin, M.

PY - 1990

Y1 - 1990

N2 - Incubation of oat root plasma membrane vesicles in the presence of ATP with trypsin or chymotrypsin increased the rate of ATP hydrolysis and ATP-dependent proton pumping by the plasma membrane H+-ATPase. Proton pumping was stimulated more than 200%, whereas ATP hydrolytic activity was stimulated about 30%. The K(m)(ATP) for both proton pumping and ATP hydrolysis was lowered from about 0.3 mM to below 0.1 mM. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of trypsin-treated plasma membranes revealed a decrease in a 100-kDa band and the appearance of a 93-kDa band. Western blot analysis using antibodies against the H+-ATPase showed that both of these bands represented the H+-ATPase and suggested that a 7-kDa segment was released. Extensive treatment with cardoxypeptidase A also activated the H+-ATPase indicating that the 7-kDa segment originated from the C terminus.

AB - Incubation of oat root plasma membrane vesicles in the presence of ATP with trypsin or chymotrypsin increased the rate of ATP hydrolysis and ATP-dependent proton pumping by the plasma membrane H+-ATPase. Proton pumping was stimulated more than 200%, whereas ATP hydrolytic activity was stimulated about 30%. The K(m)(ATP) for both proton pumping and ATP hydrolysis was lowered from about 0.3 mM to below 0.1 mM. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of trypsin-treated plasma membranes revealed a decrease in a 100-kDa band and the appearance of a 93-kDa band. Western blot analysis using antibodies against the H+-ATPase showed that both of these bands represented the H+-ATPase and suggested that a 7-kDa segment was released. Extensive treatment with cardoxypeptidase A also activated the H+-ATPase indicating that the 7-kDa segment originated from the C terminus.

UR - http://www.scopus.com/inward/record.url?scp=0025035785&partnerID=8YFLogxK

M3 - Journal article

C2 - 2143184

AN - SCOPUS:0025035785

VL - 265

SP - 13423

EP - 13426

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 23

ER -

ID: 245001434