例如："lncRNA", "apoptosis", "WRKY"

Purification and characterization of human caseinomacropeptide produced by a recombinant Saccharomyces cerevisiae.

Protein Expr. Purif.2005 Jun;41(2):441-6
{{ 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

Caseinomacropeptide (CMP) is a biologically active polypeptide derived from the C-terminal of milk kappa-casein. CMP is heterogeneous since it is modified differently by glycosylation and phosphorylation after translation. Recently, recombinant human CMP (hCMP) has been produced as a secretory product in yeast. The present study aimed at the purification and characterization of recombinant hCMP. By sequential molecular cut-off ultrafiltration and anion-exchange chromatography, the recombinant hCMP in the culture broth could be purified to an HPLC purity over 94%. The authenticity of the purified hCMP was confirmed by sequence analysis of N-terminal amino acids. The recombinant hCMP was estimated to be 7.0kDa by SDS-PAGE, and showed a lower glycosylation than the natural bovine CMP.

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

{{list.title }}

分析流程

© 2017 biocloud.net版权所有 ICP证：京10042835号