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Gewählte Publikation:

Durmus, A; Eicken, C; Spener, F; Krebs, B.
Cloning and comparative protein modeling of two purple acid phosphatase isozymes from sweet potatoes (Ipomoea batatas).
Biochim Biophys Acta. 1999; 1434(1):202-209 Doi: 10.1016/S0167-4838(99)00176-4
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Co-Autor*innen der Med Uni Graz
Spener Friedrich
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Abstract:
The sequence of cDNA fragments of two isozymes of the purple acid phosphatase from sweet potato (spPAP1 and spPAP2) has been determined by 5' and 3' rapid amplification of cDNA ends protocols using oligonucleotide primers based on amino acid information. The encoded amino acid sequences of these two isozymes show an equidistance of 72-77% not only to each other, but also to the primary structure of the purple acid phosphatase from red kidney bean (kbPAP). A three-dimensional model of the active site has been constructed for spPAP2 on the basis of the kbPAP crystallographic structure that helps to explain the reported differences in the visible and EPR spectra of spPAP2 and kbPAP.
Find related publications in this database (using NLM MeSH Indexing)
Acid Phosphatase - chemistry Acid Phosphatase - genetics
Amino Acid Sequence -
Base Sequence -
Cloning, Molecular -
DNA, Complementary - chemistry
Glycoproteins - chemistry Glycoproteins - genetics
Isoenzymes - genetics
Models, Molecular -
Molecular Sequence Data -
Plant Proteins - chemistry Plant Proteins - genetics
RNA - chemistry RNA - isolation and purification
Sequence Alignment -
Solanum tuberosum - enzymology

Find related publications in this database (Keywords)
purple acid phosphatase
sweet potato
cDNA
sequence
Ipomoea batatas
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