C.P.-D.D.-M.A.S. 13C-N.M.R. investigations of anhydrous and hydrated cyclomalto-oligosaccharides: The role of water of hydration

Hydrated and anhydrous cyclomaltohexaose, cyclomaltoheptaose, and cyclomalto-octaose (cyclodextrins) have been investigated by the c.p.-d.d.-m.a.s. ¹³C-n.m.r. technique. The chemical shifts of the signals of C-1 and C-6 provide information about conformation and the results agree fairly well with the earlier scattering data on hydrated systems, but some discrepancies have been found for cyclomaltohexaose. Th conformation of the macro-rings seems to be determined by the hydration water. The unique role of water in forming crystals of cyclomalto-oligosaccharides is demonstrated.     

XXXIV.–Notices of recent Ornithological Publications. An A. B. C. of Common Birds.

[An A. B. C. of Common Birds. A pocket guide to the commoner inland Birds of Britain. Pp. 1–04. Price 6d., by post 7d. Published by the Royal Society for the Protection of Birds, 23 Queen Anne's Gate, S.W.]     

Metabolism of monofluorobenzoates by Acinetobacter calcoaceticus N.C.I.B. 8250. Formation of monofluorocatechols.

None of the monofluorobenzoates serves as sole source of carbon and energy for growth of Acinetobacter calcoaceticus but all can contribute to growth on other substrates. The monofluorobenzoates are oxidised by bacteria pre-induced for benzoate oxidation and can themselves induce the appropriate enzymes. The initial products of oxidation have been separated and identified by gas-liquid chromatography. 2-Flurobenzoate is oxidised to catechol, fluoride and 3-fluorocatechol; 3-fluorobenzoate gives 3- and 4-fluorocatechol; 4-fluorobenzoate gives 4-fluorocatechol. The fluorocatechols appear to be partially oxidised beyond the stage of 3-oxoadipate by suitably pre-induced bacteria.     

Proteinases of Streptomyces fradiae. II. Specificity.

It has been shown that extracellular proteinases synthesized by a keratinolytic strain of S. fradiae are characterized by diversified activity in the decomposition of both proteins and synthetic substrates. Among the six proteinases isolated, apart from the ones dominating and having relatively low specificity, there are two enzymes characterized by narrow catalytic abilities--extremely similar to those of trypsin. These proteinases intensively degraded all the trypsin substrates studied, but they were inactive or showed slight activity toward others. They were also highly sensitive to such specific inhibitors of trypsin as TLCK, SBTI and TIO.