Oxygen affinities (p50) of myoglobins from four vertebrate species (Canis familiaris, rattus norvegicus, mus musculus and Gallus domesticus) as determined by a kinetic and an equilibrium method-Reference-Cited by-同舟云学术

Oxygen affinities (p50) of myoglobins from four vertebrate species (Canis familiaris, rattus norvegicus, mus musculus and Gallus domesticus) as determined by a kinetic and an equilibrium method

Published:1995-01 Issue:1 Volume:110 Page:193-199
ISSN:1096-4959
Container-title:Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology
language:en
Short-container-title:Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology

Author:

Enoki Yasunori,Matsumura Kazuhito,Ohga Yoshimi,Kohzuki Hisaharu,Hattori Masatoshi

Publisher

Elsevier BV

Subject

Molecular Biology,Physiology,Biochemistry

Reference21 articles.

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2. Interrelationship between structure and function in hemoglobin and myoglobin;Antonini;Physiol. Rev.,1965

3. The conversion of trivalent to divalent iron in hemoglobin of various species;Bauer;Analyt. Biochem.,1975

4. Spectrophotometric study of the reaction of protein -SH with organic mercurials;Boyer;J. Am. Chem. Soc.,1954

5. The reactions of the isolated α and β chains of human hemoglobin with oxygen and carbon monoxide;Brunori;J. biol. Chem.,1966

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