@article{kleszkowski_molecular_1999,
	title = {Molecular {Cloning} and {Spatial} {Expression} of an {ApL1} {cDNA} for the {Large} {Subunit} of {ADP}-{Glucose} {Pyrophosphorylase} from {Arabidopsis} thaliana},
	volume = {54},
	issn = {1865-7125},
	url = {https://www.degruyter.com/document/doi/10.1515/znc-1999-5-610/html},
	doi = {10.1515/znc-1999-5-610},
	abstract = {A cDNA, A p L 1a , corresponding to a homologue of the large subunit of ADP-glucose pyrophosphorylase (AG Pase), has been isolated/characterised by screening a cDNA library prepared from leaves of Arabidopsis thaliana, followed by rapid amplification of cDNA 3′-ends (3′-RACE). Within the 1685 nucleotide-long sequence (excluding polyA tail), an open reading frame encodes a protein of 522 amino acids (aa), with a calculated molecular weight of 57.7 kDa. The derived aa sequence does not contain any discernible transit peptide cleavage site motif, similarly to two other recently sequenced full-length Arabidopsis homo-logues for AGPase, and shows ca. 58–78 \% identity to homologous proteins from other plants/tissues. The corresponding gene was found (rosette and stem leaves, stems, flowers and fruits), consistent with its critical role in starch synthesis in},
	language = {en},
	number = {5-6},
	urldate = {2021-11-08},
	journal = {Zeitschrift für Naturforschung C},
	author = {Kleszkowski, Leszek A. and Sokolov, Lubomir N. and Luo, Cheng and Villand, Per},
	month = jun,
	year = {1999},
	note = {Publisher: De Gruyter},
	pages = {353--358},
}

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