Amino acid sequences of ferredoxins from Alocasia macrorrhiza Schott in Papua New Guinea. 1992

K Wada, and H Sakai, and R Masui, and M Ihara, and H Matsubara
Department of Biology, Faculty of Science, Kanazawa University, Ishikawa, Japan.

The amino acid sequences of ferredoxin isoproteins (Fd A and Fd B) from Alocasia macrorrhiza Schott in Papua New Guinea were determined. They consisted of single polypeptide chains of 97 and 98 residues, respectively, and both Fds had a molecular mass of 10,800 Da. There was an 88% identity between the sequences of the isoproteins (Fd A and Fd B). These sequences were compared with those of the closely related plant Fds and their phylogenetic relationships are discussed.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010219 Papua New Guinea A country consisting of the eastern half of the island of New Guinea and adjacent islands, including New Britain, New Ireland, the Admiralty Islands, and New Hanover in the Bismarck Archipelago; Bougainville and Buka in the northern Solomon Islands; the D'Entrecasteaux and Trobriand Islands; Woodlark (Murua) Island; and the Louisiade Archipelago. It became independent on September 16, 1975. Formerly, the southern part was the Australian Territory of Papua, and the northern part was the UN Trust Territory of New Guinea, administered by Australia. They were administratively merged in 1949 and named Papua and New Guinea, and renamed Papua New Guinea in 1971. New Guinea, East,New Guinea, Papua
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D010450 Endopeptidases A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS. Endopeptidase,Peptide Peptidohydrolases
D010944 Plants Multicellular, eukaryotic life forms of kingdom Plantae. Plants acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations. It is a non-taxonomical term most often referring to LAND PLANTS. In broad sense it includes RHODOPHYTA and GLAUCOPHYTA along with VIRIDIPLANTAE. Plant
D005288 Ferredoxins Iron-containing proteins that transfer electrons, usually at a low potential, to flavoproteins; the iron is not present as in heme. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed) Ferredoxin,Ferredoxin I,Ferredoxin II,Ferredoxin III
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D014644 Genetic Variation Genotypic differences observed among individuals in a population. Genetic Diversity,Variation, Genetic,Diversity, Genetic,Diversities, Genetic,Genetic Diversities,Genetic Variations,Variations, Genetic
D017386 Sequence Homology, Amino Acid The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species. Homologous Sequences, Amino Acid,Amino Acid Sequence Homology,Homologs, Amino Acid Sequence,Homologs, Protein Sequence,Homology, Protein Sequence,Protein Sequence Homologs,Protein Sequence Homology,Sequence Homology, Protein,Homolog, Protein Sequence,Homologies, Protein Sequence,Protein Sequence Homolog,Protein Sequence Homologies,Sequence Homolog, Protein,Sequence Homologies, Protein,Sequence Homologs, Protein

Related Publications

K Wada, and H Sakai, and R Masui, and M Ihara, and H Matsubara
October 2004, Archives of pharmacal research,
K Wada, and H Sakai, and R Masui, and M Ihara, and H Matsubara
February 1994, Biochimica et biophysica acta,
K Wada, and H Sakai, and R Masui, and M Ihara, and H Matsubara
November 2017, Phytochemistry,
K Wada, and H Sakai, and R Masui, and M Ihara, and H Matsubara
January 2012, Chemical & pharmaceutical bulletin,
K Wada, and H Sakai, and R Masui, and M Ihara, and H Matsubara
September 2010, Ecotoxicology and environmental safety,
K Wada, and H Sakai, and R Masui, and M Ihara, and H Matsubara
August 1975, Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
K Wada, and H Sakai, and R Masui, and M Ihara, and H Matsubara
November 2007, Journal of fluorescence,
K Wada, and H Sakai, and R Masui, and M Ihara, and H Matsubara
January 2017, Zeitschrift fur Naturforschung. C, Journal of biosciences,
K Wada, and H Sakai, and R Masui, and M Ihara, and H Matsubara
August 1977, Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
K Wada, and H Sakai, and R Masui, and M Ihara, and H Matsubara
September 1993, Biochemistry and molecular biology international,
Copied contents to your clipboard!