Journal article
CDNA cloning, characterization and expression of an endosperm-specific barley peroxidase
A barley peroxidase (BP 1) of pI ca. 8.5 and M(r) 37000 has been purified from mature barley grains. Using antibodies towards peroxidase BP 1, a cDNA clone (pcR7) was isolated from cDNA expression library. The nucleotide sequence of pcR7 gave a derived amino acid sequence identical to the 158 C-terminal amino acid residues of mature BP 1.
The clone pcR7 encodes an additional C-terminal sequence of 22 residues, which apparently are removed during processing. BP 1 is less than 50% identical to other sequenced plant peroxidases. Analyses of RNA and protein from aleurone, endosperm and embryo tissue showed maximal expression 15 days after flowering, and high levels were found only in the endosperm.
BP 1 was not expressed in the leaves.
| Language: | English |
|---|---|
| Publisher: | Kluwer Academic Publishers |
| Year: | 1991 |
| Pages: | 317-327 |
| Journal subtitle: | An International Journal on Molecular Biology, Molecular Genetics and Biochemistry |
| ISSN: | 15735028 and 01674412 |
| Types: | Journal article |
| DOI: | 10.1007/BF00020562 |
Amino Acid Sequence Biochemistry, general Cloning, Molecular DNA DNA Probes Hordeum Hordeum vulgare L. Life Sciences Molecular Sequence Data Peroxidases Plant Pathology Plant Proteins Plant Sciences Sequence Alignment amino acid sequence barley peroxidase carboxy-terminal processing cationic peroxidase glycosylation tissue-specific expression λgt11 expression library
