1965
DOI: 10.1152/jappl.1965.20.5.1041
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Solubility of krypton and xenon in blood, protein solutions, and tissue homogenates

Abstract: The solubility of krypton and xenon in human serum albumin solutions, in hemoglobin solutions, in human blood, rabbit muscle, and beef brain homogenates has been measured at 1 atm total pressure and at temperatures of 25, 30, and 37 C. The solubilities of krypton in 1 g human albumin were found to be 0.0624, 0.0412, and 0.0195 ml at 25, 30, and 37 C, respectively. The amount of xenon dissolved in 1 g human albumin was found to be 0.2382, 0.1954, and 0.1493 ml at 25, 30, and 37 C, respectively. The amount of kr… Show more

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Cited by 129 publications
(41 citation statements)
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“…Since VA, Q, and X are constant VAxe will decrease dramatically (solid line). The greatest rate of increase in Rxe (and therefore decrease in VAxe) will be when the VA/Q ratios deviate about a mean VA/Q = XXe = 0.181 (9). In the case of the very soluble gas C02 where X -9 (10), recovery is usually very high (,-0.90).…”
Section: Resultsmentioning
confidence: 99%
“…Since VA, Q, and X are constant VAxe will decrease dramatically (solid line). The greatest rate of increase in Rxe (and therefore decrease in VAxe) will be when the VA/Q ratios deviate about a mean VA/Q = XXe = 0.181 (9). In the case of the very soluble gas C02 where X -9 (10), recovery is usually very high (,-0.90).…”
Section: Resultsmentioning
confidence: 99%
“…Solubility of xenon in muscle is 0.082, and thus extremely low compared to values for middle aged adults for halothane (1.44 ± 0.17), enflurane (1.09 ± 0.10), isoflurane (1.52 ± 0.11), sevoflurane (1.08 ± 0.20), desflurane (0.62 ± 0.06), or nitrous oxide (0.54). [14][15][16] Based upon these data, it can be assumed that equilibration of xenon in the muscle compartment is complete when a steady state endexpiratory concentration has been achieved.…”
Section: Discussionmentioning
confidence: 99%
“…Hydrate stability is increased as temperatures approaeh 0° and by protein side chains whose infiuenee might conceivably vary with their degree of dissociation. Secondly, direct binding of inert gases in aqueous solutions of haemoglobin on other proteins is known to occur (Yeh and Peterson, 1965), although no specific sites have been assigned except for xenon and myoglobin (Schoenborn, Watson and Kendrew, 1965). Binding is pH dependent in the ease of bovine serum albumen (Wetlaufer and Lovrien, 1964).…”
Section: Mechanism Of Ph-effectmentioning
confidence: 99%