Eine Methode zur Ammoniakbestimmung im Capillarblut

Keller, H.; Müller-Beissenhirtz, W; Neumann, E.

doi:10.1007/bf01747105

Cited by 22 publications

(3 citation statements)

References 3 publications

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“…Ammonia was determined by slightly modifying the methods described by Seligson & Seligson (1951), Keller et al (1967), and by Rogler-Brown et al (1978), based on the Berthelot reaction.…”

Section: Methodsmentioning

confidence: 99%

Fluorescent substrate analog for adenosine deaminase: 3'-O-[5-(dimethylamino)naphthalene-1-sulfonyl]adenosine

Skorka¹,

Shuker²,

Gill³

et al. 1981

Biochemistry

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The synthesis of the fluorescent derivative of adenosine, by reaction with 5-(dimethylamino)naphthalene-1-sulfonyl chloride in dry pyridine at low temperature, yielding 3'-O-[5-(dimethylamino)naphthalene-1-sulfonyl]adenosine (3'-O-dansyladenosine), is here described. 3'-O-Dansyladenosine is partially soluble in water (approximately 10(-4) M) and upon excitation at 325 nm exhibits maximum fluorescence emission at 516 +/- 22 nm (corrected) in buffered aqueous solution at pH 7.6 with a quantum yield of 0.21 and a lifetime of 11.8 +/- 0.2 ns. The fluorescence of 3'-O-dansyladenosine is sensitive to the polarity of its solvent: in pyridine, a quantum yield of 0.61 at the emission maximum of 435 nm was observed. 3'-O-Dansyladenosine is a reversible competitive inhibitor of adenosine deaminase with a moderate inhibitive dissociation constant K1 = (1.54 +/- 0.13) X 10(-5) M. The enzyme-substrate analogue association constant was determined by equilibrium dialysis to be K = (0.69 +/- 0.05) X 10(5) M-1, very close to KI-1. The hydrophobic nature of its binding site in adenosine deaminase is evident from the strong blue shift of the fluorescence emission maximum to 440 nm, the 4-fold increase in fluorescence quantum yield, and the longer lifetime of 15.8 +/- 0.2 ns; the tight, rigid nature of the complex is evident from its high fluorescence polarization value, 0.23. An 85% decrease in the fluorescence emission intensity of the adenosine deaminase-3'-O-dansyladenosine complex in the presence of adenosine indicates the selective binding to the enzyme active site. Correlation between the conformation of the probe, either when free in various solvents or when bound to the enzyme, and its fluorescence quantum yield is noted. 3'-O-Dansyladenosine is suitable for fluorescent labeling of adenosine deaminase in cell systems.

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“…Ammonia was determined by slightly modifying the methods described by Seligson & Seligson (1951), Keller et al (1967), and by Rogler-Brown et al (1978), based on the Berthelot reaction.…”

Section: Methodsmentioning

confidence: 99%

Fluorescent substrate analog for adenosine deaminase: 3'-O-[5-(dimethylamino)naphthalene-1-sulfonyl]adenosine

Skorka¹,

Shuker²,

Gill³

et al. 1981

Biochemistry

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“…Рассчитывали артерио венозную разницу по аммиаку между артериальной кровью и кровью печеночных вен (АВР h ), между артериальной кровью и кровью почечной вены (АВР r ), порто венозную разницу по аммиаку (ПВР) -между кровью пор тальной и печеночных вен, артерио портальную разницу (АПР) -между артериальной кровью и кровью портальной ве ны. Содержание аммиака в ткани определяли микродиффузи онным методом [13], а в депротеинизированной плазме крови -фенилгипохлоридным методом [14]. Результаты обработаны статистически с учетом критериев Стьюдента и Вилкоксона.…”

Section: материал и методыunclassified

Impact of Hyperbaric Oxygenation on Ammonia Kinetics in Hepatic Failure (an Experimental Study)

Савилов¹,

Molchanov²,

Alabovsky³

2010

rmt

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“…В тканях определяли содержа ние аммиака микродиффузионным методом [5], глутамина -методом кислотного гидролиза [6] в модифика ции [5], мочевины [7]. В крови опреде ляли содержание аммиака фенилги похлоридным методом [8], глутамина [6,8], мочевины [7]. Определяли арте рио венозную (АВР), порто венозную (ПВР) и артерио портальную (АПР) разницу по аммиаку, глутамину и мо чевине.…”

Section: материалы и методыunclassified

Nitrogen Metabolism During Hepatectomy and Hyperbaric Oxygenation: Experimental Study

Савилов¹

2007

rmt

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Eine Methode zur Ammoniakbestimmung im Capillarblut

Cited by 22 publications

References 3 publications

Fluorescent substrate analog for adenosine deaminase: 3'-O-[5-(dimethylamino)naphthalene-1-sulfonyl]adenosine

Fluorescent substrate analog for adenosine deaminase: 3'-O-[5-(dimethylamino)naphthalene-1-sulfonyl]adenosine

Impact of Hyperbaric Oxygenation on Ammonia Kinetics in Hepatic Failure (an Experimental Study)

Nitrogen Metabolism During Hepatectomy and Hyperbaric Oxygenation: Experimental Study

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