1934
DOI: 10.1113/jphysiol.1934.sp003212
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The direct chemical estimation of carbamino compounds of CO2 with hæmoglobin

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1938
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Cited by 70 publications
(7 citation statements)
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“…This covalent bond causes a + 44 Da mass shift and can take place on lysine side chain amino groups [130] or at the protein's N-terminus [131] to result in the formation of a labile carbamate compound. Carbamate formation, or carbamylation, is an intrinsically rapid chemical reaction that has been shown to take place on proteins such as haemoglobin [132,133], ribulose bisphosphate carboxylase-oxygenase (RuBisCO) [134], peroxisome proteins [135] and select connexin hemichannels [136,137]. Carbamylation of these proteins has been shown to play important functional roles in regulating their activity.…”
Section: Co 2 -Dependent Post-translational Modificationsmentioning
confidence: 99%
“…This covalent bond causes a + 44 Da mass shift and can take place on lysine side chain amino groups [130] or at the protein's N-terminus [131] to result in the formation of a labile carbamate compound. Carbamate formation, or carbamylation, is an intrinsically rapid chemical reaction that has been shown to take place on proteins such as haemoglobin [132,133], ribulose bisphosphate carboxylase-oxygenase (RuBisCO) [134], peroxisome proteins [135] and select connexin hemichannels [136,137]. Carbamylation of these proteins has been shown to play important functional roles in regulating their activity.…”
Section: Co 2 -Dependent Post-translational Modificationsmentioning
confidence: 99%
“…
During the summer of 1936, unsuccessful attempts were made by J. K. W. F. and J. R. P. to measure (using the chemical method of Ferguson and Roughton, 1934) the carbamino compounds of CO 2 with hemoglobin of mackerel blood and dogfish blood. The difficulty of preparing stable solutions of hemoglobin from these bloods proved to be the most serious obstacle.
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mentioning
confidence: 99%
“…Bohr and co-workers demonstrated that the haemoglobin oxygen saturation curve was responsive to the partial pressure of CO 2 while Christiansen and co-workers showed that CO 2 uptake by the blood at constant p CO 2 was increased by the presence of O 2 2 , 3 . Henriques then used kinetic evidence to postulate the direct combination of CO 2 with the free amino groups on haemoglobin 4 and Ferguson and Roughton confirmed this through direct chemical analyses 5 . The site of CO 2 binding was demonstrated 6 , 7 to occur at the Val-1β site 8 linked to the O 2 binding state of the β-chain 9 .…”
Section: Introductionmentioning
confidence: 98%