The Complete Amino Acid Sequence for the Anaerobically Induced Aldolase from Maize Derived from cDNA Clones | Zendy

Philip M. Kelley | Zendy; Dean R. Tolan | Zendy

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The Complete Amino Acid Sequence for the Anaerobically Induced Aldolase from Maize Derived from cDNA Clones

Author(s) -

Philip M. Kelley,

Dean R. Tolan

Publication year - 1986

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.82.4.1076

Subject(s) - aldolase a , complementary dna , biology , cdna library , fructose bisphosphate aldolase , aldolase b , peptide sequence , microbiology and biotechnology , isozyme , amino acid , homology (biology) , untranslated region , biochemistry , genetics , gene , enzyme , messenger rna

A cDNA library was synthesized from maize anaerobic root mRNA and screened with cDNA specific to the anaerobically induced Zea mays cytoplasmic aldolase. At least 1% of the cDNA of the library corresponded to maize cytoplasmic aldolase. The sequence of four overlapping cDNA clones encoded a protein of molecular weight 38,611 homologous to aldolase. These cDNAs were polymorphic at three bases and one of these cDNAs had a different, shorter 3'-untranslated region. No known eukaryotic poly(A) addition site was detected. The derived amino acid sequences of maize was compared to the sequence of aldolase of trypanosome, Drosophila, and two mammalian isozymes, A and B. Of these, maize cytoplasmic aldolase was found to have the highest homology (55%) with rabbit aldolase A.

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