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Comparison of the specific activity of ribulose‐1,5‐bis‐phosphate carboxylase‐oxygenase from some C3 and C4 plants

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Comparison of the specific activity of ribulose‐1,5‐bis‐phosphate carboxylase‐oxygenase from some C3 and C4 plants. / Rintamäki, Eevi; Keys, Alfred J.; Parry, Martin A.J.
In: Physiologia Plantarum, Vol. 74, No. 2, 10.1988, p. 326-331.

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Rintamäki E, Keys AJ, Parry MAJ. Comparison of the specific activity of ribulose‐1,5‐bis‐phosphate carboxylase‐oxygenase from some C3 and C4 plants. Physiologia Plantarum. 1988 Oct;74(2):326-331. doi: 10.1111/j.1399-3054.1988.tb00638.x

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Rintamäki, Eevi ; Keys, Alfred J. ; Parry, Martin A.J. / Comparison of the specific activity of ribulose‐1,5‐bis‐phosphate carboxylase‐oxygenase from some C3 and C4 plants. In: Physiologia Plantarum. 1988 ; Vol. 74, No. 2. pp. 326-331.

Bibtex

@article{1b397292ca32482c90fcb4a45c31ee18,
title = "Comparison of the specific activity of ribulose‐1,5‐bis‐phosphate carboxylase‐oxygenase from some C3 and C4 plants",
abstract = "The specific activity of ribulose‐1,5‐bisphosphate carboxylase‐oxygenase (Rubisco, EC 4.1.1.39) was measured from the crude extracts of five C3 plants consisting of wheat (Triticum aestivum L. cv. Maris Mink), spinach (Spinacia oleracea L.), pea (Pisum sativum L. cv. Greenfeast), pumpkin (Cucurbita pepo L. cv. J{\"a}ttil{\"a}ismeloni) and Ceratodon purpureus (Hedw.) Brid., and two C4 plants, maize (Zea mays L. ETA F1) and sugar sorghum [Sorghum saccharatum (L. emend, L.) Moench]. The amount of Rubisco in the crude extracts was estimated by polyacrylamide gel electro‐phoresis with the Coomassie Brilliant Blue staining procedure. The amounts of the dye bound to the purified Rubisco of different higher plants were similar. The method gave a linear response for both purified enzyme and crude extracts, and the results agreed with those observed by immunochemical methods. The addition of positive effectors such as inorganic phosphate was necessary to obtain maximal activity in the crude extracts of all the studied plants except in that of maize. No significant differences in the specific carboxylase activity at 25°C were found between the C3 and C4 plants.",
keywords = "C plants, Ceratodon purpureus, Cucurbita pepo, inorganicphosphate, Pisum sativum, polyacrylamide gel electrophoresis, ribulose‐1,5‐bisphosphate carboxylase‐oxygenase, Rubisco, Sorghum saccharatum, specific activity, Spinacia oleracea, Triticum aestivum, Zea mays",
author = "Eevi Rintam{\"a}ki and Keys, {Alfred J.} and Parry, {Martin A.J.}",
year = "1988",
month = oct,
doi = "10.1111/j.1399-3054.1988.tb00638.x",
language = "English",
volume = "74",
pages = "326--331",
journal = "Physiologia Plantarum",
issn = "0031-9317",
publisher = "Blackwell-Wiley",
number = "2",

}

RIS

TY - JOUR

T1 - Comparison of the specific activity of ribulose‐1,5‐bis‐phosphate carboxylase‐oxygenase from some C3 and C4 plants

AU - Rintamäki, Eevi

AU - Keys, Alfred J.

AU - Parry, Martin A.J.

PY - 1988/10

Y1 - 1988/10

N2 - The specific activity of ribulose‐1,5‐bisphosphate carboxylase‐oxygenase (Rubisco, EC 4.1.1.39) was measured from the crude extracts of five C3 plants consisting of wheat (Triticum aestivum L. cv. Maris Mink), spinach (Spinacia oleracea L.), pea (Pisum sativum L. cv. Greenfeast), pumpkin (Cucurbita pepo L. cv. Jättiläismeloni) and Ceratodon purpureus (Hedw.) Brid., and two C4 plants, maize (Zea mays L. ETA F1) and sugar sorghum [Sorghum saccharatum (L. emend, L.) Moench]. The amount of Rubisco in the crude extracts was estimated by polyacrylamide gel electro‐phoresis with the Coomassie Brilliant Blue staining procedure. The amounts of the dye bound to the purified Rubisco of different higher plants were similar. The method gave a linear response for both purified enzyme and crude extracts, and the results agreed with those observed by immunochemical methods. The addition of positive effectors such as inorganic phosphate was necessary to obtain maximal activity in the crude extracts of all the studied plants except in that of maize. No significant differences in the specific carboxylase activity at 25°C were found between the C3 and C4 plants.

AB - The specific activity of ribulose‐1,5‐bisphosphate carboxylase‐oxygenase (Rubisco, EC 4.1.1.39) was measured from the crude extracts of five C3 plants consisting of wheat (Triticum aestivum L. cv. Maris Mink), spinach (Spinacia oleracea L.), pea (Pisum sativum L. cv. Greenfeast), pumpkin (Cucurbita pepo L. cv. Jättiläismeloni) and Ceratodon purpureus (Hedw.) Brid., and two C4 plants, maize (Zea mays L. ETA F1) and sugar sorghum [Sorghum saccharatum (L. emend, L.) Moench]. The amount of Rubisco in the crude extracts was estimated by polyacrylamide gel electro‐phoresis with the Coomassie Brilliant Blue staining procedure. The amounts of the dye bound to the purified Rubisco of different higher plants were similar. The method gave a linear response for both purified enzyme and crude extracts, and the results agreed with those observed by immunochemical methods. The addition of positive effectors such as inorganic phosphate was necessary to obtain maximal activity in the crude extracts of all the studied plants except in that of maize. No significant differences in the specific carboxylase activity at 25°C were found between the C3 and C4 plants.

KW - C plants

KW - Ceratodon purpureus

KW - Cucurbita pepo

KW - inorganicphosphate

KW - Pisum sativum

KW - polyacrylamide gel electrophoresis

KW - ribulose‐1,5‐bisphosphate carboxylase‐oxygenase

KW - Rubisco

KW - Sorghum saccharatum

KW - specific activity

KW - Spinacia oleracea

KW - Triticum aestivum

KW - Zea mays

U2 - 10.1111/j.1399-3054.1988.tb00638.x

DO - 10.1111/j.1399-3054.1988.tb00638.x

M3 - Journal article

AN - SCOPUS:84989682259

VL - 74

SP - 326

EP - 331

JO - Physiologia Plantarum

JF - Physiologia Plantarum

SN - 0031-9317

IS - 2

ER -