Interaction of 13CO2 and Bicarbonate with Human Hemoglobin Preparations
Formation of 13C-resonances attributable to carbamino derivatives has been observed in human erythrocyte hemolysate preparations equilibrated with 13CO2 at 33°. Carbamino formation is most marked in deoxyhemoglobin and at alkaline pH, and is very largely inhibited by the addition of 2,3-diphosphogly...
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ftpubmed:oai:pubmedcentral.nih.gov:433509 2023-05-15T18:26:46+02:00 Interaction of 13CO2 and Bicarbonate with Human Hemoglobin Preparations Morrow, Jon S. Keim, Philip Visscher, Ronald B. Marshall, Robert C. Gurd, Frank R. N. 1973-05 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC433509 http://www.ncbi.nlm.nih.gov/pubmed/4514311 en eng http://www.ncbi.nlm.nih.gov/pmc/articles/PMC433509 http://www.ncbi.nlm.nih.gov/pubmed/4514311 Biological Sciences: Biochemistry Text 1973 ftpubmed 2013-08-30T00:14:45Z Formation of 13C-resonances attributable to carbamino derivatives has been observed in human erythrocyte hemolysate preparations equilibrated with 13CO2 at 33°. Carbamino formation is most marked in deoxyhemoglobin and at alkaline pH, and is very largely inhibited by the addition of 2,3-diphosphoglycerate or conversion to oxyhemoglobin. The prominent carbamino resonance at 30.0 ppm upfield of CS2 is visible in the spectrum of packed, deoxygenated erythrocytes equilibrated in 13CO2. This chemical shift falls close to that observed with sperm-whale myoglobin and within 2 ppm upfield of that seen with simple amino acids and peptides. The bicarbonate-carbonate resonance near 33 ppm is broad in the hemoglobin preparations, which always contain some carbonic anhydrase, but becomes narrow in the presence of the carbonic anhydrase inhibitor, acetazolamide. The nuclear magnetic resonance condition of intermediate exchange rate with dissolved CO2 (68.4 ppm) obtains in the absence of inhibitor. The process has marked consequences in reducing the spin-lattice relaxation time, T1, of the bicarbonate resonance by more than 10 times. The deoxyhemoglobin carbamino resonance has a T1 value of 700 msec, indistinguishable from that of the protein carbonyl resonance envelope. Text Sperm whale PubMed Central (PMC) |
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English |
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Biological Sciences: Biochemistry |
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Biological Sciences: Biochemistry Morrow, Jon S. Keim, Philip Visscher, Ronald B. Marshall, Robert C. Gurd, Frank R. N. Interaction of 13CO2 and Bicarbonate with Human Hemoglobin Preparations |
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Biological Sciences: Biochemistry |
description |
Formation of 13C-resonances attributable to carbamino derivatives has been observed in human erythrocyte hemolysate preparations equilibrated with 13CO2 at 33°. Carbamino formation is most marked in deoxyhemoglobin and at alkaline pH, and is very largely inhibited by the addition of 2,3-diphosphoglycerate or conversion to oxyhemoglobin. The prominent carbamino resonance at 30.0 ppm upfield of CS2 is visible in the spectrum of packed, deoxygenated erythrocytes equilibrated in 13CO2. This chemical shift falls close to that observed with sperm-whale myoglobin and within 2 ppm upfield of that seen with simple amino acids and peptides. The bicarbonate-carbonate resonance near 33 ppm is broad in the hemoglobin preparations, which always contain some carbonic anhydrase, but becomes narrow in the presence of the carbonic anhydrase inhibitor, acetazolamide. The nuclear magnetic resonance condition of intermediate exchange rate with dissolved CO2 (68.4 ppm) obtains in the absence of inhibitor. The process has marked consequences in reducing the spin-lattice relaxation time, T1, of the bicarbonate resonance by more than 10 times. The deoxyhemoglobin carbamino resonance has a T1 value of 700 msec, indistinguishable from that of the protein carbonyl resonance envelope. |
format |
Text |
author |
Morrow, Jon S. Keim, Philip Visscher, Ronald B. Marshall, Robert C. Gurd, Frank R. N. |
author_facet |
Morrow, Jon S. Keim, Philip Visscher, Ronald B. Marshall, Robert C. Gurd, Frank R. N. |
author_sort |
Morrow, Jon S. |
title |
Interaction of 13CO2 and Bicarbonate with Human Hemoglobin Preparations |
title_short |
Interaction of 13CO2 and Bicarbonate with Human Hemoglobin Preparations |
title_full |
Interaction of 13CO2 and Bicarbonate with Human Hemoglobin Preparations |
title_fullStr |
Interaction of 13CO2 and Bicarbonate with Human Hemoglobin Preparations |
title_full_unstemmed |
Interaction of 13CO2 and Bicarbonate with Human Hemoglobin Preparations |
title_sort |
interaction of 13co2 and bicarbonate with human hemoglobin preparations |
publishDate |
1973 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC433509 http://www.ncbi.nlm.nih.gov/pubmed/4514311 |
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Sperm whale |
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Sperm whale |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC433509 http://www.ncbi.nlm.nih.gov/pubmed/4514311 |
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1766208734278713344 |