[Mothers in the delivery room; guidance in the use of health services].
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Biomedical subjects
Publications and source records attributed to T Takagi.
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An indirect method, based on the analysis of metal contents, for the determination of metallothionein (MT) in body fluids is described. Affinity chromatography gel was used as a solid phase extraction (SPE) support for preconcentration of MT Proteins and metals bound to MT from spiked water and human urine samples. The results showed a good correlation between the concentration of MT proteins added to water or physiological human urine and the concentration of protein indirectly determined by atomic absorption spectrometry (AAS) recovered by the SPE-affinity chromatography technique and calculated from the metal concentration. The present method can be used in toxicological analysis for determination of MT concentration in physiological fluids in subjects exposed to heavy metals.
Electrophoretic mobilities of various proteins or peptides complexed with sodium dodecyl sulfate (SDS) were determined by free solution capillary electrophoresis. The complexes formed between SDS and protein polypeptide showed electrophoretic mobilities virtually insensitive to the protein molecular weight. On the other hand, scattered and larger negative electrophoretic mobilities were observed for peptides of molecular weights less than 10000. Mobility differences as small as 0.3-3% among the three differently modified derivatives of bovine serum albumin could also be successfully determined due to the high resolving power of capillary electrophoresis.