The purpose of the study is to purify human growth hormone from the
fermentation broth by affinity chromatography. For this purpose, human growth
hormone specific oligonucleotide aptamers are selected among an aptamer
library / selected oligonucleotides were synthesized and used as ligands. Effect of
pH on ligand-human growth hormone complex formation was investigated and
the highest complex formation was obtained at pH= 7.0. Human growth hormone
is separated from the fermentation broth with 99.8% purity and 41% overall
yield. The equilibrium data obtained was described by Langmuir type isotherm
where saturation constant (q0) and affinity constant (K) are calculated as 0.338
mg hGH/ì / mol aptamer and 0.059 mg hGH/ml, respectively. Further, equilibriumdata obtained using aptamer affinity column was described by Langmuir type
isotherm where saturation constant (q0) and affinity constant (K) are 0.027 mg
hGH/ì / mol aptamer and 1.543 mg hGH/ml, respectively. It is possible that,
selected aptamer can be used for purification of bulk amounts of recombinant
human growth hormone by using aptamer affinity chromatography.
| Identifer | oai:union.ndltd.org:METU/oai:etd.lib.metu.edu.tr:http://etd.lib.metu.edu.tr/upload/12613911/index.pdf |
| Date | 01 February 2008 |
| Creators | Balci, Oguz |
| Contributors | Calik, Pinar |
| Publisher | METU |
| Source Sets | Middle East Technical Univ. |
| Language | English |
| Detected Language | English |
| Type | Ph.D. Thesis |
| Format | text/pdf |
| Rights | To liberate the content for public access |
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