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Literature DB >> 17391

The kinetics of the recombination reaction between apomyoglobin and alkaline haematin.

Abstract

Apomyoglobin was prepared by an extremely mild modification of the acid/butanone technique, and the kinetics of the recombination reaction between this preparation and alkaline haematin were studied. The recombination has been shown to be precisely second-order and mono-phasic. Rate constants obtained from the study are in good agreement with values obtained previously by an indirect technique not involving separation of haem and apoprotein.

Entities: Chemical

Mesh：

Substances：

Year: 1977 PMID： 17391 PMCID： PMC1164671 DOI： 10.1042/bj1630153

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

15 in total

1. The kinetics and mechanism of the recombination reaction between apomyoglobin and haemin.

Authors: P A Adams
Journal: Biochem J Date: 1976-11 Impact factor: 3.857

2. CHANGES IN SIDE CHAIN REACTIVITY ACCOMPANYING THE BINDING OF HEME TO SPERM WHALE APOMYOGLOBIN.

Authors: E BRESLOW
Journal: J Biol Chem Date: 1964-02 Impact factor: 5.157

3. THE COMBINATION OF PORPHYRINS WITH NATIVE HUMAN GLOBIN.

Authors: Q H GIBSON
Journal: J Biol Chem Date: 1964-10 Impact factor: 5.157

4. REVERSIBLE CONFORMATIONAL CHANGES OF MYOGLOBIN AND APOMYOGLOBIN.

Authors: S C HARRISON; E R BLOUT
Journal: J Biol Chem Date: 1965-01 Impact factor: 5.157

5. [Thermodynamic study of the heme-globin association. I. Dissociation equilibrium of metmyoglobin: thermodynamic data].

Authors: R BANERJEE
Journal: Biochim Biophys Acta Date: 1962-10-22

6. Cleavage of the haem-protein link by acid methylethylketone.

Authors: F W TEALE
Journal: Biochim Biophys Acta Date: 1959-10

7. Kinetic studies on the reaction between native globin and haem derivatives.

Authors: Q H GIBSON; E ANTONINI
Journal: Biochem J Date: 1960-11 Impact factor: 3.857

8. Studies on the structure of hemoglobin. I. Physicochemical properties of human globin.

Authors: A R FANELLI; E ANTONINI; A CAPUTO
Journal: Biochim Biophys Acta Date: 1958-12

9. Metal replaced hemoproteins. A review with introductory laboratory preparation of cobaltmyoglobin.

Authors: L C Dickinson
Journal: J Chem Educ Date: 1976-06 Impact factor: 2.979

10. Studies on cytochrome c peroxidase. IX. The reaction of ferrimyoglobin with hydroperoxides and a comparison of peroxide-induced compounds of ferrimyoglobin and cytochrome c peroxidase.

Authors: T Yonetani; H Schleyer
Journal: J Biol Chem Date: 1967-04-25 Impact factor: 5.157

9 in total

1. Effects of pH on the kinetic reaction mechanism of myoglobin unfolding studied by time-resolved electrospray ionization mass spectrometry.

Authors: O O Sogbein; D A Simmons; L Konermann
Journal: J Am Soc Mass Spectrom Date: 2000-04 Impact factor: 3.109

The kinetics of the recombination reaction between apomyoglobin and alkaline haematin.

1. The kinetics and mechanism of the recombination reaction between apomyoglobin and haemin.

2. CHANGES IN SIDE CHAIN REACTIVITY ACCOMPANYING THE BINDING OF HEME TO SPERM WHALE APOMYOGLOBIN.

3. THE COMBINATION OF PORPHYRINS WITH NATIVE HUMAN GLOBIN.

4. REVERSIBLE CONFORMATIONAL CHANGES OF MYOGLOBIN AND APOMYOGLOBIN.

5. [Thermodynamic study of the heme-globin association. I. Dissociation equilibrium of metmyoglobin: thermodynamic data].

6. Cleavage of the haem-protein link by acid methylethylketone.

7. Kinetic studies on the reaction between native globin and haem derivatives.

8. Studies on the structure of hemoglobin. I. Physicochemical properties of human globin.

9. Metal replaced hemoproteins. A review with introductory laboratory preparation of cobaltmyoglobin.

10. Studies on cytochrome c peroxidase. IX. The reaction of ferrimyoglobin with hydroperoxides and a comparison of peroxide-induced compounds of ferrimyoglobin and cytochrome c peroxidase.

1. Effects of pH on the kinetic reaction mechanism of myoglobin unfolding studied by time-resolved electrospray ionization mass spectrometry.

2. Diffusion measurements by electrospray mass spectrometry for studying solution-phase noncovalent interactions.

3. Folding and assembly of hemoglobin monitored by electrospray mass spectrometry using an on-line dialysis system.

4. Interaction of macrophage-migration-inhibitory factor with haematin.

5. Respiration triggers heme transfer from cytochrome c peroxidase to catalase in yeast mitochondria.

6. Picosecond fluorescence decay of tryptophans in myoglobin.

7. Fluorescence and energy transfer of tryptophans in Aplysia myoglobin.

8. A simple three-dimensional-focusing, continuous-flow mixer for the study of fast protein dynamics.

9. BODIPY-Based Fluorescent Probes for Sensing Protein Surface-Hydrophobicity.