Effects of ATP and Zn2+ on degradation of the large subunit of ribulose-1, 5-bisphosphate carboxylase/oxygenase in wheat leaves

No abstract is available for this paper.

• Publication year

  2012

• Venue

  African Journal of Agricultural Research

• Publication date

  2012-02-05

• Fields of study

  Biology, Environmental Science

• Identifiers
  DOI 10.5897/AJAR11.1789
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar

• No claims are published for this paper.

• No concepts are published for this paper.

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  2002cited by this paper
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  1998cited by this paper
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  1997cited by this paper
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  1997cited by this paper
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  1996cited by this paper
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  1996cited by this paper
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  1996cited by this paper
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  1996cited by this paper
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  1995cited by this paper
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  1995cited by this paper
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  1995cited by this paper
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  1995cited by this paper
• Nitrogen Metabolism in Senescing Leaves

  1994cited by this paper
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  1993cited by this paper
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  1993cited by this paper
• Characterization of a prolyl endopeptidase from spinach thylakoids

  1992cited by this paper
• Characteristics of ribulose-1,5-bisphosphate carboxylase/oxygenase degradation by lysates of mechanically isolated chloroplasts from wheat leaves.

  1990influential reference
• Proteolytic activity during senescence of plants.

  1990cited by this paper
• Endopeptidases in the stroma and thylakoids of pea chloroplasts.

  1989cited by this paper
• Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa.

  1987cited by this paper
• [15] Isolation of intact chloroplasts: General principles and criteria of integrity

  1987cited by this paper
• Cleavage of structural proteins during

  1970cited by this paper

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