SO-CAETID fermentation lactic acids are generally believed to be inactive, since it was ascertained by Phelps & Palmer [1917] and Pederson et al. [1926] that optically inactive lactic acid was produced in many natural fermentations. The lactic acid in Sake was found to be the inactive form, although not only inactive lactic acid-producing organisms (Lactobacillus sake), but also optically activ...

The utilization of glycogen by skeletal muscle was, at one time, one of the central problems of biochemistry. Attention focused on the most dramatic property of the system: the very rapid glycogenolysis that occurs synchronously with muscle contraction. This phenomenon now has a generally accepted explanation : the increase in Ca2+ that induces muscle contraction also activates phosphorylase ki...

Gold(i) catalyses the ring-opening addition of cyclopropenes in a mild and regioselective manner.

Cytoplasmic thioltransferase purified from rat liver [Axelsson, Eriksson & Mannervik (1978) Biochemistry 17, 2978--2984] catalyses the formation and decomposition of mixed disulphides of proteins and glutathione. The enzyme was found to catalyse the reversible thiol-disulphide interchange between glutathione disulphide and a crude thiol-containing protein fraction from rat liver. This finding i...

Rat heart mitochondria respiring on succinate in the presence of Ruthenium Red (to inhibit uptake on the Ca2+ uniporter) released Ca2+ on the calcium/sodium antiporter until a steady state was reached. Addition of the ionophore A23187 (which catalyses Ca2+/2H+ exchange) did not perturb this steady state. Thermodynamic analysis showed that if a Ca2+/nNa+ exchange with any value of n other than 2...

FIH (Factor inhibiting hypoxia-inducible factor), an asparaginyl beta-hydroxylase belonging to the super-family of 2-oxoglutarate and Fe(II)-dependent dioxygenases, catalyses hydroxylation of Asn-803 of hypoxia-inducible factor, a transcription factor that regulates the mammalian hypoxic response. Only one other asparaginyl beta-hydroxylase, which catalyses hydroxylation of both aspartyl and as...