Science in English encyclopædias, 1704–1875.—II

The Reverend Dr John Beale, FRS, DD, and chaplain to Charles II, carried out a vigorous campaign in the early Royal Society for the reform of agriculture, trade, and public education-reforms which signalled his continuing commitment to the ideas not only of Bacon, but of Hartlib and Comenius as well. In addition to promoting orchard plantations and expanded commercial horticulture, he collaborated with Evelyn, Oldenburg, and Houghton to publish or publicize items on the improvement of agriculture and the national economy. His later writings, including the unfinished manifesto ‘From Utopia’, also identify the ‘mercantilist’ thought of Thomas Mun as a crucial link in Beale's alignment of technology, socioeconomic reform, and the religious and ethical values of Christian humanism.     

Pattern of nucleotide substitution at major histocompatibility complex class I loci reveals overdominant selection

The major histocompatibility complex (MHC) loci are known to be highly polymorphic in humans, mice and certain other mammals, with heterozygosity as high as 80-90% (ref. 1). Four different hypotheses have been proposed to explain this high degree of polymorphism: (1) a high mutation rate, (2) gene conversion or interlocus genetic exchange, (3) over dominant selection and (4) frequency-dependent selection. In an attempt to establish which of these hypotheses is correct, we examined the pattern of nucleotide substitution between polymorphic alleles in the region of the antigen recognition site (ARS) and other regions of human and mouse class I MHC genes. The results indicate that in ARS the rate of nonsynonymous (amino acid altering) substitution is significantly higher than that of synonymous substitution in both humans and mice, whereas in other regions the reverse is true. This observation, together with a theoretical study and other considerations, supports the hypothesis of overdominant selection (heterozygote advantage).     

Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation

Haemolysin secreted by pathogenic Escherichia coli binds to mammalian cell membranes, disrupting cellular activities and lysing cells by pore-formation. It is synthesized as nontoxic prohaemolysin (proHlyA), which is activated intracellularly by a mechanism dependent on the cosynthesized HlyC. Haemolysin is one of a family of membrane-targeted toxins, including the leukotoxins of Pasteurella and Actinobacillus and the bifunctional adenylate cyclase haemolysin of Bordetella pertussis, which require this protoxin activation 1-5. HlyC alone cannot activate proHlyA, but requires a cytosolic activating factor6. Here we report the cytosolic activating factor is identical to the acyl carrier protein and that activation to mature toxin is achieved by the transfer of a fatty acyl group from acyl carrier protein to proHlyA. Only acyl carrier protein, not acyl-CoA, can promote HlyC-directed proHlyA acylation, but a range of acyl groups are effective.     

Serotonin storage mechanism and its interaction with reserpine

Zusammenfassung Es gelang nicht, mit physikalisch-chemischen Methoden einen HT-Komplex in hämolysierten oder homogenisierten Suspensionen von Kaninchen-Thrombozyten nachzuweisen. Versuchsergebnisse über die HT-Aufnahme durch Thrombozyten stimmen mit der Möglichkeit überein, dass das Amin in den Zellen durch einen aktiven Transportmechanismus konzentriert wird. Es wird angenommen, dass die Abgabe von normalem HT aus der Zelle unter Reserpineinwirkung, durch eine Hemmung des Aufnahmemechanismus und langsame, passive Diffusion aus den Zellen erfolgt.