Improved high-speed de-excitation system for brushless synchronous machines tested on a 20 MVA hydro-generator

Synchronous machines with brushless excitation have the disadvantage that the field winding is not accessible for the de-excitation of the machine. This means that, despite the proper operation of the protection system, the slow de-excitation time constant may produce severe damage in the event of an internal short circuit. A high-speed de-excitation system for these machines was developed, and this study presents the continuation of a previously published study. This study presents the design by computer simulation and the results of the first commissioning of this de-excitation system in a commercial 20 MVA hydro-generator. The de-excitation is achieved by inserting resistance in the field circuit, obtaining a dynamic response similar to that achieved in machines with static excitation. In this case, a non-linear discharge resistor was used, making the dynamic response even better.

The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein– protein interactions independent of carbohydrate moiety

The lecticans are a family of chondroitin sulfate proteoglycans including aggrecan, versican, neurocan, and brevican. The C-terminal globular domains of lecticans are structurally related to selectins, consisting of a C-type lectin domain flanked by epidermal growth factor and complement regulatory protein domains. The C-type lectin domain of versican has been shown to bind tenascin-R, an extracellular matrix protein specifically expressed in the nervous system, and the interaction was presumed to be mediated by a carbohydrate–protein interaction. In this paper, we show that the C-type lectin domain of brevican, another lectican that is specifically expressed in the nervous system, also binds tenascin-R. Surprisingly, this interaction is mediated by a protein–protein interaction through the fibronectin type III domains 3–5 of tenascin-R, independent of any carbohydrates or sulfated amino acids. The lectin domains of versican and other lecticans also bind the same domain of tenascin-R by protein–protein interactions. Surface plasmon resonance analysis revealed that brevican lectin has at least a 10-fold higher affinity than the other lectican lectins. Tenascin-R is coprecipitated with brevican from adult rat brain extracts, suggesting that tenascin-R and brevican form complexes in vivo. These results demonstrate that the C-type lectin domain can interact with fibronectin type III domains through protein–protein interactions, and suggest that brevican is a physiological tenascin-R ligand in the adult brain.