Powered by OpenAIRE graph
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Biochemistry and Cel...arrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
Biochemistry and Cell Biology
Article . 1997 . Peer-reviewed
License: CSP TDM
Data sources: Crossref
Biochemistry and Cell Biology
Article . 1997 . Peer-reviewed
Data sources: Crossref
versions View all 3 versions

Molecular cloning and expression of avian smooth muscle S100A11 (calgizzarin, S100C)

Authors: B O, Schönekess; M P, Walsh;

Molecular cloning and expression of avian smooth muscle S100A11 (calgizzarin, S100C)

Abstract

S100A11 (calgizzarin or S100C), a member of the S100 family of Ca2+-binding proteins, was first identified in chicken gizzard smooth muscle and subsequently detected in several mammalian species and tissues. We now report the full-length coding sequence of avian smooth muscle S100A11. The cloned nucleotide sequence is 515 bases in length, which includes in-frame start and stop codons and encodes a protein of 101 amino acids. The chicken S100A11 sequence differs from human S100A11 at 25 positions (9 conserved) and is four residues shorter (overall identity 72.4%, similarity 81%). The protein contains two EF hands and conserved hydrophobic residues involved in dimer formation. Cloned avian S100A11 expressed in Escherichia coli and purified by Ca2+-dependent hydrophobic interaction chromatography and ion-exchange chromatography was recognized by polyclonal antibodies raised against tissue-purified protein and, like tissue-purified S100A11, bound 45Ca2+ in a gel overlay assay. Key words: S100A11, calgizzarin, Ca2+-binding protein, smooth muscle, avian.

Related Organizations
Keywords

Base Sequence, Swine, Calcium Radioisotopes, Calcium-Binding Proteins, Immunoblotting, Molecular Sequence Data, S100 Proteins, Muscle, Smooth, Mice, Gizzard, Avian, Animals, Humans, Calcium, Amino Acid Sequence, Rabbits, Cloning, Molecular, Chickens, Protein Binding

  • BIP!
    Impact byBIP!
    citations
    This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
    14
    popularity
    This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
    Average
    influence
    This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
    Top 10%
    impulse
    This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
    Average
Powered by OpenAIRE graph
citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
14
Average
Top 10%
Average