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Digitale Medien

Somatosensory evoked potentials in patients with hypocalcaemia after parathyroidectomy (1988)

Kanda, F. ; Jinnai, J. ; Fujita, T.

Springer

Journal of neurology 235 (1988), S. 136-139

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ISSN: 1432-1459

Schlagwort(e): Parathyroidectomy ; Hypoparathyroidism ; Hypocalcaemia ; Somatosensory evoked potentials ; Recovery functions

Quelle: Springer Online Journal Archives 1860-2000

Thema: Medizin

Notizen: Summary The effects of hypocalcaemia on somatosensory evoked potentials (SEPs) were studied in five patients after parathyroidectomy. Despite normal latencies the mean value of amplitudes of the SEPs in hypocalcaemic patients was greater than that in normocalcaemic subjects. Recovery functions of the SEPs showed a significant decrease in hypocalcaemic patients at interstimulus intervals of about 10 ms compared with those in normocalcaemic patients and in normal volunteers. Recovery functions appear to be a valid indicator of synaptic efficacy, especialy for evaluation of the reduction in conduction efficacy of the central nervous system in hypocalcaemia.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF00314302

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Digitale Medien

Structural analysis of protein variants by mass spectrometry: Characterization of haemoglobin providence using a grand-scale mass spectrometer (1989)

Wada, Y. ; Fujita, T. ; Hayashi, A. ; [weitere]

Chichester : Wiley-Blackwell

Biological Mass Spectrometry 18 (1989), S. 563-565

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Details

ISSN: 0887-6134

Schlagwort(e): Chemistry ; Analytical Chemistry and Spectroscopy

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Chemie und Pharmazie

Notizen: A grand-scale mass spectrometer with high mass resolution and high transmission was employed for the analysis of haemoglobin variant. Two variants were isolated from a haemolysate by chromatography. Secondary ion mass spectrometry of complex peptide mixtures derived from these variants precisely determined the molecular weight of abnormal peptides. The molecular weight, 2857.4 and 2858.4, indicated the amino acid substitutions of asparagine and aspartic acid, respectively, for lysine at position 82 of β globin chain. The mutations had been reported in haemoglobin Providence.

Zusätzliches Material: 2 Ill.