Ribulose-1,5-bis-Phosphate Carboxylase/Oxygenase Degradation in Isolated Pea Chloroplasts Incubated in the Light or in the Dark

Mitsuhashi, Wataru; Crafts-Brandner, Steven J.; Feller, Urs (1992). Ribulose-1,5-bis-Phosphate Carboxylase/Oxygenase Degradation in Isolated Pea Chloroplasts Incubated in the Light or in the Dark. Journal of Plant Physiology, 139(6), pp. 653-658. Elsevier 10.1016/S0176-1617(11)81706-2

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Intact pea (Pisum sativum L.) chloroplasts isolated mechanically were incubated in the dark or in the light. After incubation intact chloroplasts were reisolated on Percoll steps prior to analysis. A 37 kD polypeptide derived from the large subunit of ribulose-1,5-bis-phosphate carboxylase/oxygenase accumulated during incubation in darkness. Other degradation products (45, 42, 37, and 32 kD) were detected on immunoblots from organelles incubated in the light. The catabolism of Rubisco in the chloroplasts was affected by the composition of the incubation medium.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Other Institutions > Emeriti, Faculty of Science
08 Faculty of Science > Department of Biology > Institute of Plant Sciences (IPS) > Plant nutrition [discontinued]
08 Faculty of Science > Department of Biology > Institute of Plant Sciences (IPS)

UniBE Contributor:

Feller, Urs

Subjects:

500 Science > 580 Plants (Botany)

ISSN:

0176-1617

Publisher:

Elsevier

Language:

English

Submitter:

Peter Alfred von Ballmoos-Haas

Date Deposited:

27 Jan 2017 09:42

Last Modified:

08 May 2018 15:03

Publisher DOI:

10.1016/S0176-1617(11)81706-2

Uncontrolled Keywords:

Pisum sativum L., chloroplast, illumination, proteolysis, ribulose-1,5-bis phosphate carboxylase/oxygenase

BORIS DOI:

10.7892/boris.91903

URI:

https://boris.unibe.ch/id/eprint/91903

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