PMID: 5911536Mar 1, 1966

Camel myoglobin

The Biochemical Journal
E S Awad, L Kotite

Abstract

1. Crystalline myoglobin was prepared from camel heart muscle. 2. A method was developed for the isolation of myoglobin that employs molecular-sieve chromatography. 3. Analytical chromatography of the camel myoglobin on a molecular-sieve column and on two types of ion-exchange columns gave in each case a single elution band, which accounted for better than 98% recovery and showed that the product was free from haemoglobin. 4. The iron content on a dry weight basis was 0.308%. This value corresponds to a molecular weight of 18100. 5. The spectra of acidic ferrimyoglobin, basic ferrimyoglobin and ferrimyoglobin cyanide were measured. 6. The pK(a) of the dissociation of the haem-bound water molecule in acidic ferrimyoglobin was 8.53 at 25 degrees . 7. Conclusions are drawn about the charge on the surface of the camel ferrimyoglobin molecule as compared with horse and sperm-whale ferrimyoglobins.

Citations

Aug 1, 1969·European Journal of Biochemistry·A H Van den OordJ A Verheij

Related Concepts

Artiodactyla
Chromatography
Ion-Exchange Chromatography Procedure
Polymorphism, Crystallization
Myocardium
Myoglobin
Spectrophotometry
Physicochemical Phenomena

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