例如:"lncRNA", "apoptosis", "WRKY"

Studies on cytochrome-c oxidase, XIII. Amino-acid sequence of the small membrane polypeptide VIIIc from bovine heart respiratory complex IV.

Biol. Chem. Hoppe-Seyler. 1986 Jan;367(1):67-73. doi:10.1515/bchm3.1986.367.1.67
{{ author.authorName }}{{getOrganisationIndexOf(author)}} {{ author.authorName }}{{getOrganisationIndexOf(author)}}
{{ author.authorName }}{{getOrganisationIndexOf(author)}} {{ author.authorName }}{{getOrganisationIndexOf(author)}}
+ et al

[No authors listed]

Author information
  • {{index+1}} {{ organisation }}

摘要


The isolation and complete amino-acid sequence analysis of the cytoplasmically synthesized polypeptide VIIIc from bovine heart cytochrome-c oxidase is described. The protein is a stoichiometric constituent of the mitochondrial respiratory complex IV. Its primary structure is deduced from N-terminal sequencing and peptides obtained by enzymatic cleavage with Staphylococcus aureus proteinase and chemical cleavage with cyanogen bromide. The small protein consists of 56 amino acids summing up to a total Mr of 6243. From position 34 to 51 the chain contains a hydrophobic sequence of 18 residues. This probably membrane-spanning segment also contains the 2 cysteine residues of the chain. The function of this subunit in the respiratory complex IV is still unknown.

KEYWORDS: {{ getKeywords(articleDetailText.words) }}

基因功能


  • {{$index+1}}.{{ gene }}

图表


原始数据


 保存测序数据
Sample name
Organism Experiment title Sample type Library instrument Attributes
{{attr}}
{{ dataList.sampleTitle }}
{{ dataList.organism }} {{ dataList.expermentTitle }} {{ dataList.sampleType }} {{ dataList.libraryInstrument }} {{ showAttributeName(index,attr,dataList.attributes) }}

文献解读