Complete amino acid sequence for human aldolase B derived from cDNA and genomic clones.
Open Access
- 1 May 1984
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 81 (9) , 2738-2742
- https://doi.org/10.1073/pnas.81.9.2738
Abstract
Several aldolase B clones from a human liver c[complementary]DNA library were identified by using a rabbit aldolase A cDNA as a hybridization probe. The most complete of these, pHL413, is 1389 base pairs long and covers .apprxeq. 80% of the length of the m[messenger]RNA, including 90% of the translated region. The cDNA, pHL413, was used to identify a genomic clone, .lambda.HG313, which encoded the remaining amino acids of human aldolase B. The amino acid and nucleotide sequences of aldolase are strongly conserved even between different isozymes. In the 3''-untranslated regions of the mRNA for the B isozyme of human and rat there is an extensive stretch of homology. Aldolase B lacks a cysteine at positions 72 and 338 and lacks a histidine at position 361. These residues, which are present in rabbit aldolase A, were previously proposed to take part in catalysis. This may not be the case.This publication has 37 references indexed in Scilit:
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