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Digitale Medien

OCCURRENCE OF A SEROTONIN SULPHOTRANSFERASE IN THE BRAIN (1969)

Hidaka, H. ; Nagatsu, T. ; Yagi, K.

Oxford, UK : Blackwell Publishing Ltd

Journal of neurochemistry 16 (1969), S. 0

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ISSN: 1471-4159

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Medizin

Notizen: Abstract— —An enzyme catalysing the transfer of sulphate from 3′-phosphoadenylsulphate to serotonin was purified from rabbit brain. The purification procedure involved ammonium sulphate fractionation of the 200,000 g supernatant of rabbit brain homogenate, treatment with alumina Cγ, and chromatography on DEAE-cellulose. The enzyme was purified 67-fold from the 200,000 g supernatant of the brain homogenate. The intracranial distribution of the sulphotransferase was investigated and the cerebellum found to have rather high activity. The sulphotransferase activities of rabbit, dog, rat and bovine brains were compared; rabbit brain had the highest activity, followed by dog, rat and bovine brain.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1111/j.1471-4159.1969.tb06457.x

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Digitale Medien

Poly(3-hydroxybutyrate) as an endogeneous substrate for H 2 evolution in Rhodovulum sulfidophilum (1997)

Maeda, I. ; Idehara, K. ; Okayama, N. ; [weitere]

Springer

Biotechnology letters 19 (1997), S. 1209-1212

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ISSN: 1573-6776

Quelle: Springer Online Journal Archives 1860-2000

Thema: Werkstoffwissenschaften, Fertigungsverfahren, Fertigung

Notizen: Abstract In the absence of an external substrate, H 2 was evolved in Rhodovulum sulfidophilum under light-anaerobic conditions, along with degradation of poly(3-hydroxybutyrate) (PHB). Cells grown with succinate as a sole carbon source accumulated only a small amount of PHB compared with that in cells grown with a multiple substrate consisting of a mixture of four organic acids. Unlike PHB-containing cells, PHB-deficient cells did not evolve H in the absence of an external substrate. Nitrogenase activity was expressed while no hydrogenase activity was detected during the incubation of PHB-containing cells. These results suggest that intracellular PHB serves as a substrate for the H evolution catalyzed by nitrogenase when an external substrate is lacking.