PMID: 11328592May 1, 2001Paper

Characterization of cytochrome b(5) in the ascidian Polyandrocarpa misakiensis and budding-specific expression

Journal of Biochemistry
T YubisuiKazuo Kawamura

Abstract

A cDNA for cytochrome b(5) was cloned from a cDNA library of buds of the ascidian, Polyandrocarpa misakiensis, by a hybridization method involving a digoxigenin-labeled cDNA probe of human soluble cytochrome b(5). The nucleotide sequence of the cDNA for the ascidian cytochrome b(5) (Pmb5) consisted of about 1,800 base pairs including 5'- and 3'-noncoding regions, and a coding sequence of 405 base pairs. The amino acid sequence of 135 residues deduced from the coding nucleotide sequence exhibited 54% identity and 76% similarity to chicken cytochrome b(5). A highly conserved amino acid sequence was observed in the amino-terminal domain of 96 residues containing two heme-binding histidine residues. The putative soluble form of the recombinant Pmb5 expressed in Escherichia coli was purified to homogeneity by column chromatographies on an anion-exchanger and gel filtration. The purified Pmb5 showed the typical absorption spectrum of cytochrome b(5) with an asymmetric peak at 556 nm and a shoulder at 560 nm upon reduction with NADH and NADH-cytochrome b(5) reductase. The low temperature spectrum of the dithionite-reduced form of the protein contained the split peaks at 551 and 555 nm, this spectrum being very similar to that of mamma...Continue Reading

Citations

Mar 30, 2004·Journal of Biochemistry·Toshitsugu YubisuiKazuo Kawamura
May 29, 2010·Development, Growth & Differentiation·Nagamoto KanekoShigeki Fujiwara
Mar 8, 2007·Bioscience, Biotechnology, and Biochemistry·Terumi IkegamiToshitsugu Yubisui

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