[50] Physical methods for the study of myoglobin

Autor: Frank R. N. Gurd, T. Michael Rothgeb
Rok vydání: 1978
Předmět:
DOI: 10.1016/s0076-6879(78)52052-1
Popis: Publisher Summary This chapter outlines the methods of isolation and characterization of myoglobins, spectral properties in different heme ligand states, titration and stability properties, oxygen binding equilibrium, and analysis of dynamic phenomena related to myoglobins. The full interpretation of the dynamic processes requires close analysis of the properties of myoglobins from related species to correlate both functional and evolutionary relationships with other carriers and enzymes in the oxidative pathway of muscle. Myoglobins are isolated from skeletal muscle, and sometimes from heart muscle, of a considerable number of animal species. The close structural similarity to the individual hemoglobin chains in the characteristic globin fold has served to maintain the focus of attention on this protein. Similar to hemoglobin, myoglobin was early recognized to have structural similarities among species and has contributed to the important concepts of the preservation of secondary structure in protein evolution and the development of functional domains.
Databáze: OpenAIRE