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Publication
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| Research Title |
the study of oxygen affinity of cross-linked crocodile (Crocodylus siamensis) hemoglobin |
| Date of Distribution |
11 July 2017 |
| Conference |
| Title of the Conference |
The 5th Asia Pasific Protein Association ()APPA Conference and The 12th International Symposium of The Protein Society of Thailand (PST) |
| Organiser |
International Symposium of The Protein Society of Thailand (PST) |
| Conference Place |
The Tide resort, Bangsan |
| Province/State |
Chonburi |
| Conference Date |
11 July 2017 |
| To |
14 July 2017 |
| Proceeding Paper |
| Volume |
2017 |
| Issue |
1 |
| Page |
149 |
| Editors/edition/publisher |
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| Abstract |
A variety of cross-linked cell-free hemoglobin (CL-Hb) compounds have been developed with the aim of creating novel hemoglobin based oxygen carriers (HBOCs). The main purpose of Hb crosslinking is to increase the stability of the native tetrameric form of hemoglobin when it circulates in the bloodstream in order to prevent low serum half-life and renal toxicity, while still retaining its function as an oxygen transporter protein. However, the derived CL-Hb using different cross-linking agents exhibits a lower oxygen affinity than native hemoglobin. Therefore, crocodile (C. siamensis) hemoglobin (cHb) constitutes an interesting new approach in HBOC development, as it was reported to possess a higher oxygen affinity than human hemoglobin (hHb). In this study, cHb was cross-linked at 4°C for 2 h with glutaraldehyde at different concentrations (0.025%, 0.050%, 0.075%, 0.100%, 0.125% and 0.150%). It is important to note that SDS-PAGE results show an apparent reduction of only the α-monomer band when the glutaraldehyde concentration was increased and that protein bands with a high molecular weight (>45 kDa) were observed. Moreover, the CL-cHbs present P50 values (mmHg) and Hills coefficients (Values in parentheses) of 12.244 (n=1.781), 14.614 (n=2.153), 16.983 (n=2.327), 12.759 (n=1.736), 12.420 (n=2.831) and 13.863 (n=2.360), respectively. All results indicate a lower oxygen affinity than that of native cHb, which has a P50 of 6.855 (n= 2.763), while being not significantly different from native hHb. In conclusion, cHb represents a highly interesting alternative to human Hb used in the production of conventional cross-linked cell-free hemoglobin, since it exhibits oxygen binding characteristics that may benefit the development of a cHb-based oxygen carrier suitable for human use in the future. |
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| Peer Review Status |
มีผู้ประเมินอิสระ |
| Level of Conference |
นานาชาติ |
| Type of Proceeding |
Abstract |
| Type of Presentation |
Poster |
| Part of thesis |
true |
| Presentation awarding |
false |
| Attach file |
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| Citation |
0
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Journal Publication
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