[47] Hemoglobin porphyrin modification
Methods in Enzymology, ISSN: 0076-6879, Vol: 52, Issue: C, Page: 447-455
1978
- 26Citations
- 2Captures
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Metrics Details
- Citations26
- Citation Indexes26
- 26
- CrossRef21
- Captures2
- Readers2
Article Description
This chapter provides information on hemoglobin porphyrin modification. Generally, hemoglobin porphyrin modifications are performed in four steps, which are (1) preparation of globin, (2) chemical modification of hemes and porphyrins, (3) recombination of globin with modified hemes, and (4) purification of the reconstituted hemoglobin. Hemoglobin in red blood cells and myoglobin in muscle are important oxygen-carrying hemoproteins consisting of an oxygen-binding group, heme, and globin. Neither heme nor globin combines with oxygen reversibly; therefore, this function of hemoglobin and myoglobin must be related to the interaction between heme and globin. An excellent technique for the study of this interaction is the chemical modification of the heme in hemoglobin. Combination of globin with hemin is a physiological process in vivo because these two components are known to be synthesized separately in the cells. In addition, it is possible to investigate the effect of electron distribution of the heme on the ligand affinity and optical property of hemoglobin by using various reconstituted hemoglobins.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0076687978520491; http://dx.doi.org/10.1016/s0076-6879(78)52049-1; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0017831242&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/672647; http://linkinghub.elsevier.com/retrieve/pii/S0076687978520491; https://linkinghub.elsevier.com/retrieve/pii/S0076687978520491; http://dx.doi.org/10.1016/s0076-6879%2878%2952049-1; https://dx.doi.org/10.1016/s0076-6879%2878%2952049-1
Elsevier BV
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