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 c...
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ftpubmed:oai:pubmedcentral.nih.gov:1264936 2023-05-15T18:26:43+02:00 Camel myoglobin Awad, E. S. Kotite, L. 1966-03 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1264936 http://www.ncbi.nlm.nih.gov/pubmed/5911536 en eng http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1264936 http://www.ncbi.nlm.nih.gov/pubmed/5911536 Articles Text 1966 ftpubmed 2013-08-30T16:15:17Z 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 pKa of the dissociation of the haem-bound water molecule in acidic ferrimyoglobin was 8·53 at 25°. 7. Conclusions are drawn about the charge on the surface of the camel ferrimyoglobin molecule as compared with horse and sperm-whale ferrimyoglobins. Text Sperm whale PubMed Central (PMC) |
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Articles Awad, E. S. Kotite, L. Camel myoglobin |
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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 pKa of the dissociation of the haem-bound water molecule in acidic ferrimyoglobin was 8·53 at 25°. 7. Conclusions are drawn about the charge on the surface of the camel ferrimyoglobin molecule as compared with horse and sperm-whale ferrimyoglobins. |
format |
Text |
author |
Awad, E. S. Kotite, L. |
author_facet |
Awad, E. S. Kotite, L. |
author_sort |
Awad, E. S. |
title |
Camel myoglobin |
title_short |
Camel myoglobin |
title_full |
Camel myoglobin |
title_fullStr |
Camel myoglobin |
title_full_unstemmed |
Camel myoglobin |
title_sort |
camel myoglobin |
publishDate |
1966 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1264936 http://www.ncbi.nlm.nih.gov/pubmed/5911536 |
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Sperm whale |
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Sperm whale |
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1264936 http://www.ncbi.nlm.nih.gov/pubmed/5911536 |
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