MR-Radix: a multi-relational data mining algorithm

Abstract Background Once multi-relational approach has emerged as an alternative for analyzing structured data such as relational databases, since they allow applying data mining in multiple tables directly, thus avoiding expensive joining operations and semantic losses, this work proposes an algorithm with multi-relational approach. Methods Aiming to compare traditional approach performance and multi-relational for mining association rules, this paper discusses an empirical study between PatriciaMine - an traditional algorithm - and its corresponding multi-relational proposed, MR-Radix. Results This work showed advantages of the multi-relational approach in performance over several tables, which avoids the high cost for joining operations from multiple tables and semantic losses. The performance provided by the algorithm MR-Radix shows faster than PatriciaMine, despite handling complex multi-relational patterns. The utilized memory indicates a more conservative growth curve for MR-Radix than PatriciaMine, which shows the increase in demand of frequent items in MR-Radix does not result in a significant growth of utilized memory like in PatriciaMine. Conclusion The comparative study between PatriciaMine and MR-Radix confirmed efficacy of the multi-relational approach in data mining process both in terms of execution time and in relation to memory usage. Besides that, the multi-relational proposed algorithm, unlike other algorithms of this approach, is efficient for use in large relational databases.

Jacalin interaction with human immunoglobulin A1 and bovine immunoglobulin G1: Affinity constant determined by piezoelectric biosensoring

The affinity of the d-galactose-binding lectin from Artocarpus heterophyllus lectin, known as jacalin, with immonuglobulins (Igs) was determined by biofunctionalization of a piezoelectric transducer. This piezoelectric biofunctionalized transducer was used as a mass-sensitive analytical tool, allowing the real-time binding analysis of jacalin-human immunoglobulin A1 (IgA(1)) and jacalin-bovine IgG(1) interactions from which the apparent affinity constant was calculated. The strategy was centered in immobilizing jacalin on the gold electrode's surface of the piezoelectric crystal resonator using appropriate procedures based on self-assembling of 11-mercaptoundecanoic acid and 2-mercaptoethanol thiol's mixture, a particular immobilization strategy by which it was possible to avoid cross-interaction between the proteins over electrode's surface. The apparent affinity constants obtained between jacalin-human IgA(1) and jacalin-bovine IgG(1) differed by 1 order of magnitude [(8.0 +/- 0.9) x 10(5) vs (8.3 +/- 0.1) x 10(6) L mol(-1)]. On the other hand, the difference found between human IgA(1) and human IgA(2) interaction with jacalin, eight times higher for IgA(1), was attributed to the presence of O-linked glycans in the IgA(1) hinge region, which is absent in IgA(2). Specific interaction of jacalin with O-glycans, proved to be present in the human IgA(1) and hypothetically present in bovine IgG(1) structures, is discussed as responsible for the obtained affinity values.