Camel myoglobin

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Abstract
Crystalline myoglobin was prepared from camel heart muscle. A method was developed for the isolation of myoglobin that employs molecular-sieve chromatography. Analytical chromatography of the camel myoglobin on a molecular-sieve column and on 2 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 hemoglobin. The iron content on a dry weight basis was 0.308%. This value corresponds to a molecular weight of 18,100. The spectra of acidic ferrimyoglobin, basic ferri-myoglobin and ferrimyoglobin cyanide were measured. The pKa of the dissociation of the heme-bound water molecule in acidic ferrimyoglobin was 8. 53 at 25[degree]. 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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