Health Dictionary
Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.
Myoglobinuria historical perspective
Introduction
Discovery
Discovery
- In 1958 John Kendrew and associates announced that they have discovered that Myoglobin was the first protein to have its three-dimensional structure revealed by X-ray crystallography.[1] .[2]
- For this discovery, John Kendrew shared the 1962 Nobel Prize in chemistry with Max Perutz.[3]
Landmark Events in the Development of Treatment Strategies
Landmark Events in the Development of Treatment Strategies
- Despite being one of the most studied proteins in biology, its physiological function is not yet conclusively established: mice genetically engineered to lack myoglobin can be viable and fertile but show many cellular and physiological adaptations to overcome the loss. Through observing these changes in myoglobin-deplete mice, it is hypothesised that myoglobin function relates to increased oxygen transport to muscle, oxygen storage and as a scavenger of reactive oxygen species.[4]
References
References
- ↑ (U.S.) National Science Foundation: Protein Data Bank Chronology (Jan. 21, 2004). Retrieved 3.17.2010
- ↑ Kendrew JC, Bodo G, Dintzis HM, Parrish RG, Wyckoff H, Phillips DC (Mar 1958). “A three-dimensional model of the myoglobin molecule obtained by x-ray analysis”. Nature. 181 (4610): 662–6. Bibcode:1958Natur.181..662K. doi:10.1038/181662a0. PMID 13517261.
- ↑ The Nobel Prize in Chemistry 1962
- ↑ Garry DJ, Kanatous SB, Mammen PP (2007). “Molecular insights into the functional role of myoglobin”. Advances in Experimental Medicine and Biology. 618: 181–93. doi:10.1007/978-0-387-75434-5_14. PMID 18269197.