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Author

E. Antonini

Bio: E. Antonini is an academic researcher from Rockefeller Foundation. The author has contributed to research in topics: Globin. The author has an hindex of 1, co-authored 1 publications receiving 577 citations.
Topics: Globin

Papers
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Journal ArticleDOI
TL;DR: The most important physicochemical constants of human globin and its coupling capacity for hematin are reported.

578 citations


Cited by
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Journal ArticleDOI
TL;DR: In this paper, anilino-8-naphthalene sulfonate (ANS) was used as a fluorescent probe of non-polar regions in proteins and its fluorescence changes markedly when it is bound to the apoprotein.

1,420 citations

Book ChapterDOI
TL;DR: This chapter describes hemoglobin and myoglobin, and briefly describes some properties and reactions of their prosthetic group, mainly because the characteristic physiological functions of these proteins arise from the intrinsic reactivity of the heme.
Abstract: Publisher Summary This chapter describes hemoglobin and myoglobin. Hemoglobin and myoglobin are, among all proteins, ones that have been, and are, most actively studied; an enormous number of papers have been published over the past hundred years on all aspects of their properties and behavior. The study of these proteins has gone beyond the interest in their physiological role as oxygen carriers because they represent ideal models for investigating the properties of proteins in general, especially of enzymes. Correspondingly, current knowledge of the structure and function of hemoglobin and myoglobin is far greater than that available for any other protein. In spite of this, however, many questions still remain unsolved regarding the exact molecular mechanisms involved in the function of these proteins. Before discussing the properties of respiratory heme proteins, it is necessary to briefly describe some properties and reactions of their prosthetic group, mainly because the characteristic physiological functions of these proteins arise from the intrinsic reactivity of the heme.

491 citations

Journal ArticleDOI
TL;DR: Intact heme groups undergo exchange between molecules of human hemoglobin under physiological conditions, although at equilibrium the affinity of human albumin for ferriheme is only about one-fifteenth that of globin.

395 citations