Literature DB >> 3395128

The primary structure of chicken liver cytochrome b5 deduced from the DNA sequence of a cDNA clone.

H Zhang1, C Somerville.   

Abstract

A cDNA clone encoding the chicken liver cytochrome b5 was isolated by probing a library with synthetic oligonucleotides based on a partial amino acid sequence of the protein. Determination of the DNA sequence indicated a 414-nucleotide open reading frame which encodes a 138-amino acid residue polypeptide. The open reading frame contains 6 amino acids at the amino terminus which were not present on any of the cytochrome b5 polypeptides for which the amino acid sequence has been determined directly, suggesting that the protein is proteolytically processed to the mature form. The results of genomic Southern analysis were consistent with the presence of two structurally different genes in the chicken genome, raising the possibility that the soluble and membrane-bound forms of the protein are the products of separate genes.

Entities:  

Mesh:

Substances:

Year:  1988        PMID: 3395128     DOI: 10.1016/0003-9861(88)90603-0

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN: 0003-9861            Impact factor:   4.013


  2 in total

1.  In vitro membrane-inserted conformation of the cytochrome b(5) tail.

Authors:  M R Hanlon; R R Begum; R J Newbold; D Whitford; B A Wallace
Journal:  Biochem J       Date:  2000-11-15       Impact factor: 3.857

2.  The carboxy-terminal 10 amino acid residues of cytochrome b5 are necessary for its targeting to the endoplasmic reticulum.

Authors:  J Mitoma; A Ito
Journal:  EMBO J       Date:  1992-11       Impact factor: 11.598

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.