Camel myoglobin.

E S Awad; L Kotite

doi:10.1042/bj0980909

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Camel myoglobin.

E S Awad·L Kotite

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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.

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Animals Artiodactyla Chemical Phenomena Chemistry, Physical Chromatography Chromatography, Ion Exchange Crystallization In Vitro Techniques Myocardium Myoglobin Spectrophotometry Journal Article

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E S Awad, L Kotite. 1966. Camel myoglobin.. https://doi.org/10.1042/bj0980909

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