Skip Navigation

This Article
Right arrow Print PDF (901K)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (32)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Yang, F.
Right arrow Articles by Bowman, B. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yang, F.
Right arrow Articles by Bowman, B. H.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1985, Vol. 13, No. 22 8007-8017
© 1985

Articles

Evolutionary and structural relationships among the group-specific component, albumin and {alpha}-fetoprotein

Funmei Yang, Victor J. Luna, Robert D. McAnelly, Kathleen H. Naberhaus, Rod L. Cupples and Barbara H. Bowman

Department of Cellular and Structural Biology, University of Texas Health Science Centerat San Antonio 7703 Floyd Curl Drive, San Antonio, TX 78284, USA

Received August 28, 1985. Accepted October 21, 1985.

The group-specific component (Gc) is a plasma protein that binds vitamin D. Recent characterization of human Gc cDNA demonstrated homology with serum albumin and {alpha}-fetoprotein. This study compares the sequences of the three proteins and demonstrates a strong evolutionary relationship. Albumin, {alpha}-fetoprotein and Gc evolved from an ancestral gene containing an intragenic triplication. Comparison of the amino acid sequences and patterns of double disulfide bonds suggests that the Gc gene may have diverged from an ancestral gene earlier in evolution than the genes encoding albumin and {alpha}-fetoprotein. Analysis of the amino acid and nucleotide sequences of the three internal domains of Gc revealed 19–23% amino acid sequence identity and the localization of three homology blocks with 40–44% nucleotide sequence identity. The deduced amino sequence of Gc furnished data for comparing its molecular configuration based on the predicted secondary structure with those predicted form human albumin and {alpha}-fetoprotein. Utilization of Gc cDNA has also led to the identification of its genomic DNA and detectioin of a human DNA polymorphism.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Exp. Biol. Med.Home page
G. J. Mizejewski
Alpha-fetoprotein Structure and Function: Relevance to Isoforms, Epitopes, and Conformational Variants
Experimental Biology and Medicine, May 1, 2001; 226(5): 377 - 408.
[Abstract] [Full Text]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.