Abstract
The complete amino acid sequence of human skeletal myoglobin is described. That of heart myoglobin is found by homology to be the same. When myoglobin is prepared some minor fractions may be obtained besides the main component. They are shown to be artefacts arising from deamidations. The likely three-dimensional structure of human myoglobin is discussed, taking that of sperm-whale myoglobin as a reference. Human myoglobin is compared with the
α
- and
β
-chains of human haemoglobin. There is a noteworthy similarity of internal residues and haem contacts, but little resemblance of sites where the haemoglobin chains form dimeric and tetrameric contacts, when they become subunits of the haemoglobin molecule.
Reference17 articles.
1. tkeson A. & Theorell H . i960 On th e m icroheterogeneity of horse m yoglobin. Archs Biochem. B iophys.91 319-325.
2. tkeson A. E h ren stein V. H evesy G. & Theorell H . i960 Life span of myoglobin. Archs Biochem. B iophys. 91 310-318.
3. P ro tein coagulation an d its reversal. The p rep aratio n of insoluble globin, soluble globin an d hem e. J . gen;Physiol.,1930
4. Effects of a Ititu d e acclim atization on ra t m yoglobin. Changes in m yoglobin co n ten t of skeletal an d cardiac muscle. A m;Physiol.,1959
5. R eactions colorees specifiques de l 'arginine et de la tyrosine realisees apres chrom atographie su r papier. Biochim. biophys;Ircher E .;Acta,1952
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