Camel myoglobin.
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.
D000818:Animals; D001188:Artiodactyla; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002845:Chromatography; D002852:Chromatography, Ion Exchange; D003460:Crystallization; D066298:In Vitro Techniques; D009206:Myocardium; D009211:Myoglobin; D013053:Spectrophotometry
D009211:Myoglobin