Positive alliesthesia after insulin.

Volunteers experienced sucrose solution as more pleasant 36-48 min after insulin, than after saline control. These changes in affective estimates correlate negatively with blood sugar at 30 min and positively at 50 min after the insulin injection.     

Positive alliesthesia after insulin

Summary Volunteers experienced sucrose solution as more pleasant 36–48 min after insulin, than after saline control. These changes in affective estimates correlate negatively with blood sugar at 30 min and positively at 50 min after the insulin injection.     

The effect of insulin on the electrophoretic mobility of rat hepatocytes

The addition of insulin (10 microU) to a suspension of isolated hepatocytes in Krebs-Ringer bicarbonate solution, causes an increase in the negative electrophoretic mobility of the cells from - 1.68 micrometer sec-1 V-1 cm to 2.26 micrometer sec-1 V-1 cm. This observation supports the findings by other workers that the binding of insulin to its receptor leads to a marked change in the membrane.     

The pre-raphaelites and science

Classic voltaic batteries of the silver/zinc and copper/zinc types are the ancestors of today's primary cells, and facilitated the development of many aspects of electrical technology. Nevertheless, they appear never to have been studied and evaluated in a quantitative manner, with results recorded in terms of volts, amps, ohms, and watts. Research of this nature is reported here, and has been conducted for the most part with copper/zinc cells. Log–log graphs of voltage versus load and current, and power versus load, are presented for many electrolyte systems. It has been shown that, although the textbook electrolyte of dilute sulphuric acid does work, it is an order of magnitude inferior to a solution containing some additional nitric acid. The latter diminishes the current‐limiting phenomenon of polarization, and was in fact used by Davy, Faraday, and other early investigators. A quantitative consideration of Nicholson and Carlisle's discovery of the electrolysis of water with a silver/zinc voltaic pile is followed by examination of the electrolysis of pure water, trough batteries, and Davy's isolation of potassium and sodium. Every battery gives maximum power when its resistance is adjusted (by appropriate series/parallel connections) to match the resistance of the load: the maximum output of the ‘Great Battery’ of the Royal Institution is assessed at no more than 3 kW. The paper concludes with a note on the recognized hazard of long‐term exposure to mercury vapour (produced by amalgamation of zinc electrodes in batteries) and its possible relevance to the health of Michael Faraday.     

Medium- and short-chain dehydrogenase/reductase gene and protein families

Zinc plays an important role in the structure and function of many enzymes, including alcohol dehydrogenases (ADHs) of the MDR type (mediumchain dehydrogenases/reductases). Active site zinc participates in catalytic events, and structural site zinc maintains structural stability. MDR-types of ADHs have both of these zinc sites but with some variation in ligands and spacing. The catalytic zinc sites involve three residues with different spacings from two separate protein segments, while the structural zinc sites involve four residues and cover a local segment of the protein chain (Cys97-Cys111 in horse liver class I ADH). This review summarizes properties of both ADH zinc sites, and relates them to zinc sites of proteins in general. In addition, it highlights a separate study of zinc binding peptide variants of the horse liver ADH structural zinc site. The results show that zinc coordination of the free peptide differs markedly from that of the enzyme (one His / three Cys versus four Cys), suggesting that the protein zinc site is in an energetically strained conformation relative to that of the peptide. This finding is a characteristic of an entatic state, implying a functional nature for this zinc site.     

Zinc binding to peptide analogs of the structural zinc site in alcohol dehydrogenase: Implications for an entatic state

Zinc binding to the peptide replica and analogs to residues 93–115 of horse liver alcohol dehydrogenase (ADH) was examined by competition of the peptides and the chromophoric chelator 4-(2- pyridylazo)resorcinol for zinc and X-ray absorption fine structure analysis of the zinc ligands. In the enzyme, zinc is coordinated by four Cys residues. In the peptide replica, zinc is bound to three Cys and one His residue. A four-Cys zinc coordination is observed only when His is removed, leading to increased zinc stability. ADH crystal structures reveal that the ε-amino group of the conserved residue Lys323 is within H-bond distance of the backbone amide oxygens of residues 103, 105 and 108, likely stabilizing the zinc coordination in the enzyme. The peptide data thus indicate structural strain and increased energy in the zinc-binding site in the protein, characteristic of an entatic state, implying a functional nature for this zinc site. Received 3 July 2008; received after revision 11 August 2008; accepted 1 September 2008     

Role of Cys221 and Asn116 in the zinc-binding sites of the Aeromonas hydrophila metallo-β-lactamase

The CphA metallo--lactamase produced by Aeromonas hydrophila exhibits two zinc-binding sites. Maximum activity is obtained upon binding of one zinc ion, whereas binding of the second zinc ion results in a drastic decrease in the hydrolytic activity. In this study, we analyzed the role of Asn116 and Cys221, two residues of the active site. These residues were replaced by site-directed mutagenesis and the different mutants were characterized. The C221S and C221A mutants were seriously impaired in their ability to bind the first, catalytic zinc ion and were nearly completely inactive, indicating a major role for Cys221 in the binding of the catalytic metal ion. By contrast, the binding of the second zinc ion was only slightly affected, at least for the C221S mutant. Mutation of Asn116 did not lead to a drastic decrease in the hydrolytic activity, indicating that this residue does not play a key role in the catalytic mechanism. However, the substitution of Asn116 by a Cys or His residue resulted in an approximately fivefold increase in the affinity for the second, inhibitory zinc ion. Together, these data suggested that the first zinc ion is located in the binding site involving the Cys221 and that the second zinc ion binds in the binding site involving Asn116 and, presumably, His118 and His196.Received 3 March 2003; received after revision 4 August 2003; accepted 25 August 2003