Purification and identification of recombiant human IGF-Ⅰ / 军事医学科学院院刊
Bulletin of The Academy of Military Medical Sciences
;
(6): 129-132, 2001.
Article
in Chinese
| WPRIM
| ID: wpr-642446
ABSTRACT
Objective:
To obtain highly purified recombinant human IGF-Ⅰ(rhIGF-Ⅰ) and identify it.Methods:
rhIGF-Ⅰ Was purified through ion-exchange chromatography and gel filtration chromatography after the inclusion bodies of rhIGF-Ⅰ were extracted from Escherichia coli. The recombinant protein was characterized through molecular weight assay, Western-blot, and fluorescent chromatography. The renaturation and biological assay of rhIGF-Ⅰ were investigated. Results andConclusions:
The purity of rhIGF-Ⅰ was higher than 99%. The analysis of molecular weight, Western-blot, fluorescent chromatography and sequences of NH2-terminal 15 amino acids were same as those anticipated. 3-10 mg/ml was the concentration of renatured rhIGF-Ⅰ to support half-maximal stimulation of cell proliferation with BALB/c 3T3 cells.
Full text:
Available
Index:
WPRIM (Western Pacific)
Type of study:
Diagnostic study
Language:
Chinese
Journal:
Bulletin of The Academy of Military Medical Sciences
Year:
2001
Type:
Article
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