Plan lecithin: cholesterol acyltransferases

Multicellular living organisms and unmodified parts thereof and – Plant – seedling – plant seed – or plant part – per se

Reexamination Certificate

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Details

C435S069100, C435S468000, C435S183000, C435S235100, C435S325000, C435S410000, C435S419000, C435S252300, C435S320100, C530S370000, C536S023200, C536S023600, C800S278000, C800S295000

Reexamination Certificate

active

06940003

ABSTRACT:
This invention relates to an isolated nucleic acid fragment encoding a plant lecithin: cholesterol acyltransferases. The invention also relates to the construction of a chimeric gene encoding all or a portion of the plant lecithin:cholesterol acyltransferases in sense or antisense orientation, wherein expression of the chimeric gene results in production of altered levels of the plant lecithin:cholesterol acyltransferases in a transformed host cell.

REFERENCES:
patent: 98/46767 (1998-10-01), None
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EMBL Sequence Database Library Accession No.: AC004557, Apr. 15, 1998, P. Shinn et al., Genomic sequence for Arabidopsis thaliana BAC F17L21.
Craig H. Warden et al., J. Biol. Chem., vol. 264(36):21573-21581, 1989, Tissue-specific Expression, Developmental Regulation, and Chromosomal mapping of the lecithin: cholesterol acyltransferase gene.
Yukio Murata et al., J. Lipid Res., vol. 37:1616-1622, 1996, Cloning of rabbit LCAT cDNA:increase in LCAT mRNA abundance in the liver of cholesterol-fed rabbits.
EMBL Sequence Database Library Accession No.: AW147120, Nov. 4, 1999, V. Walbot, Maize ESTs from various cDNA libraries sequenced at stanford University.
National Center for Biotechnology Information General Identifier No. 998999, Sep. 27, 1995, P.A. Schindler et al., Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
Patrick A. Schindler et al., Protein Science, vol. 4:791-803, 1995, Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
National Center for Biotechnology Information General Indentifier No. 418623, Jun. 11, 1999, G. Meroni et al., Nucleotide sequence of the cDNA for lecithin:cholesterol acyltransferase (LCAT) from the rat.
G. Meroni et al., Nucl. Acids Res., vol. 18(17):5308, Nucleotide sequence of the cDNA for lecithin:cholesterol acyltransferase (LCAT) from the rat.
Jotun Hein, Meth. in Enzymol., vol. 183:626-645, 1990, Unified approach to alignment and phyogenise.
National Center for Biotechnology Information General Identifier No: 3935185, Dec. 1, 1998, P. Shinn et al., Genomic sequence for Arabidopsis thaliana BAC F17L21.
Mitsuhisa Manabe et al., J. Lipid Res., vol. 28:1206-1215, 1987, New substrate for determination of serum lecithin: cholesterol acyltransferase.
Sissel Rogne et al., The Isolation And Characterisation Of A cDNA Clone For Human Lecithin:Cholesterol Acyl Transferase And Its Use To Analyse The Genes in Patients With LCAT Deficiency And Fish Eye Disease, Biochemical and Biophysical Research Communications, vol. 148:161-169, 1987.

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