Application of Special Arresters on 138 kV Lines of Application Power Company
Special zinc oxide series gapped line arresters were installed on Appalachian Power Company 138 kV lines having high tower footing resistance and severe lightning exposure. This effort was part of an experiment to explore means of reducing lightning flashovers in exposed locations where low ground resistances are not feasible. Because of possible future voltage uprating of these lines, the arresters were built in the form of high strength nonporcelain mechanical struts, designed to limit phase conductor swing. This paper describes the field installation of these experimental arresters and their instrumentation and reports operating experience in 1983.
Expulsion protective gaps on 132 kv lines
Discussion of a paper by Philip Spom and I. W. Gross published in the January 1935 issue, pases 66–73, and presented for oral discussion at the general overhead line problems session of the winter convention, New York, N. Y., January 23, 1935. Other discussions of this paper were published in the March 1935 issue, pases 329–32.
Comparative studies of α-Lactalbumin and lysozyme: Echidna lysozyme
Summaryα-Lactalbumin is a modifier protein for galactosyl transferase in the biosynthesis of lactose and lysozyme catalyses the cleavage of β(1–4) glycosidic linkages. It is now generally believed that α-lactalbumin and lysozyme have diverged from a common ancestor. Comparative studies of these proteins from several species are reported here.The presence of lactose and lactose synthetase activity is shown in mature milk samples from a variety of placental mammals (eutheria) and a pouch bearing mammal (marsupialia). The isolation of the α-lactalbumins involved and their properties are compared.The position is different in the milk samples of monotremes. The α-lactalbumin, lactose and lactose synthetase activity levels in the two platypus samples studied are very low. The levels of lactose and lactose synthetase activity in some echidna(Tachyglossus aculeatus) samples are low, but appreciable in others. No α-lactalbumin is present. The lysozyme activity is appreciable, some samples containing a different lysozyme from that present in others. One of these (designated echidna lysozyme I) is capable of lactose synthetase modifier activity in the presence of bovine “A protein”.The properties of this lysozyme are compared with those of lysozymes and α-lactalbumins from a variety of species and their significance is discussed.