Nucleotide and deduced amino acid sequence of a pu...[Biochim Biophys Acta. 1994]

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1: Biochim Biophys Acta. 1994 Dec 30;1224(3):463-6.Links

Nucleotide and deduced amino acid sequence of a putative higher molecular weight precursor for catalase in sunflower cotyledons.

Kleff S, Trelease RN, Eising R.

University of Münster, Department of Botany, Germany.

A cDNA from a sunflower (Helianthus annuus L.) library encoded a 56.8 kDa catalase peptide. N-terminal sequence comparisons to peroxisomal higher molecular weight precursors revealed conserved amino acid motifs around the (putative) cleavage sites. These findings suggest that the 55 kDa catalase in sunflower cotyledons is synthesized at a higher molecular weight.

PMID: 7803505 [PubMed - indexed for MEDLINE]

The predominant protein in peroxisomal cores of sunflower cotyledons is a catalase that differs in primary structure from the catalase in the peroxisomal matrix. [Eur J Biochem. 1997]
Amino acid and cDNA sequences of a methionine-rich 2S protein from sunflower seed (Helianthus annuus L.). [Eur J Biochem. 1991]
Isolation and expression pattern of hahr1, a homeobox-containing cDNA from Helianthus annuus. [Gene. 1997]
A cDNA encoding a putative lipid transfer protein expressed in sunflower seeds. [J Plant Physiol. 2003]
Cloning, expression, and purification of glyoxysomal 3-oxoacyl-CoA thiolase from sunflower cotyledons. [Protein Expr Purif. 2004]

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Nucleotide and deduced amino acid sequence of a putative higher molecular weight precursor for catalase in sunflower cotyledons.

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