Managing effective partnerships in older people's services

The integration of older people's services is a challenge to all countries with an ageing population. Although it is widely acknowledged that acute care, long-term care, social care, housing, leisure, education and other services should all operate in a more 'joined-up manner', achieving this in practice remains extremely difficult. Against this background, the European Union (EU) Care and Management of Services for Older People in Europe Network (CARMEN) project set out to explore the management of integrated care in 11 EU countries. Summarising key themes from the project, this paper explores the management of integrated care, the skills required, the mechanisms which aid successful integrated approaches, and future research priorities. Although very challenging, the concept of integrated care is still a promising way forward when seeking to meet the challenges of an ageing society

Catalytic and Molecular Properties of the Quinohemoprotein Tetrahydrofurfuryl Alcohol Dehydrogenase from Ralstonia eutropha Strain Bo

The quinohemoprotein tetrahydrofurfuryl alcohol dehydrogenase (THFA-DH) from Ralstonia eutropha strain Bo was investigated for its catalytic properties. The apparent k(cat)/K(m) and K(i) values for several substrates were determined using ferricyanide as an artificial electron acceptor. The highest catalytic efficiency was obtained with n-pentanol exhibiting a k(cat)/K(m) value of 788 × 10(4) M(−1) s(−1). The enzyme showed substrate inhibition kinetics for most of the alcohols and aldehydes investigated. A stereoselective oxidation of chiral alcohols with a varying enantiomeric preference was observed. Initial rate studies using ethanol and acetaldehyde as substrates revealed that a ping-pong mechanism can be assumed for in vitro catalysis of THFA-DH. The gene encoding THFA-DH from R. eutropha strain Bo (tfaA) has been cloned and sequenced. The derived amino acid sequence showed an identity of up to 67% to the sequence of various quinoprotein and quinohemoprotein dehydrogenases. A comparison of the deduced sequence with the N-terminal amino acid sequence previously determined by Edman degradation analysis suggested the presence of a signal sequence of 27 residues. The primary structure of TfaA indicated that the protein has a tertiary structure quite similar to those of other quinoprotein dehydrogenases