Die Jod131-Markierung von Insulin, ACTH und STH mit hoher spezifischer Aktivität zur Anwendung in der radioimmunologischen Methode

Melani, F; Bartelt, K. M.; Conrads, R.; Pfeiffer, E. F.

doi:10.1515/cclm.1966.4.4.189

Cited by 3 publications

(2 citation statements)

References 2 publications

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“…We used a modified technique of 131I-labelling according to Melani et al [26] which yielded LDHX and LDH5 enzyme preparations with a high specific radioactivity (incorporation rate, 45% of 131I), and nearly without loss of enzyme activity (95% yield). Unfortunately, even these preparations proved to be unstable in vivo.…”

Section: Discussion Of Methods and Materialsmentioning

confidence: 99%

Studies on Enzyme Elimination

U¹,

Friedel²,

Heine³

et al. 1972

Enzyme

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The fate of 14C-LDH5 after intravenous and intraperitoneal injection was studied in dogs and rats. The enzyme was labelled by means of incorporating 14C-acetate groups into the enzyme protein. The turnover of extracellular 14C-LDH5 was investigated by measurement of 14C-radioactivity, enzyme activity, and by autoradiography. The elimination of 14C-LDH5 takes place in the intravascular space, as well as in the extravascular fluid compartments. Part of the 14C-LDH(5)-radioactivity is excreted in urine, bile, and the gastrointestinal tract; a smaller amount remains in the organism. A specific elimination organ cannot be distinguished, as the enzyme elimination is multilocal. The significance of enzyme elimination in the diagnostic assessment of enzyme levels in serum is indicated. The labeling of enzymes with isotopes and the behavior of cell enzymes in the extracellular compartment are discussed, and the results are compared with other results in the literature.

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Section: Discussion Of Methods and Materialsmentioning

confidence: 99%

Studies on Enzyme Elimination

U¹,

Friedel²,

Heine³

et al. 1972

Enzyme

View full text Add to dashboard Cite

show abstract

“…The problem could be solved by the use of radioactively labelled enzymes which would remain traceable after inactivation and even after resumption into cells or excretion. With regard to in rive experiments labelling of e-amino groups with [14C]acetate [45,46] was found to be more suitable than labelling by 131iodine [47][48][49][50][51]. Not only is the yield of catalytically active enzyme after labelling many times better, but, aside from the expected minor alteration of the electrophoretic mobility, kinetic and molecular properties remain unaltered; further, the stability is excellent in vitro as well as in vivo.…”

Section: E 62mentioning

confidence: 99%