On diagonal-Schur complements of block diagonally dominant matrices

It is known that the diagonal-Schur complements of strictly diagonally dominant matrices are strictly diagonally dominant matrices [J.Z. Liu, Y.Q. Huang, Some properties on Schur complements of H-matrices and diagonally dominant matrices, Linear Algebra Appl. 389 (2004) 365-380], and the same is true for nonsingular H-matrices [J.Z. Liu, J.C. Li, Z.T. Huang, X. Kong, Some properties of Schur complements and diagonal-Schur complements of diagonally dominant matrices, Linear Algebra Appl. 428 (2008) 1009-1030]. In this paper, we research the properties on diagonal-Schur complements of block diagonally dominant matrices and prove that the diagonal-Schur complements of block strictly diagonally dominant matrices are block strictly diagonally dominant matrices, and the same holds for generalized block strictly diagonally dominant matrices. (C) 2010 Elsevier Inc. All rights reserved.

Lung alveolar proteomics of bronchoalveolar lavage from a pulmonary alveolar proteinosis patient using high-resolution FTICR mass spectrometry

High-resolution Fourier transform ion cyclotron resonance (FTICR) mass spectrometry was developed and applied to the proteome analysis of bronchoalveolar lavage fluid (BALF) from a patient with pulmonary alveolar proteinosis. With use of 1-D and 2-D gel electrophoresis, surfactant protein A (SP-A) and other surfactant-related lung alveolar proteins were efficiently separated and identified by matrix-assisted laser desorption/ionization FTICR mass spectrometry . Low molecular mass BALF proteins were separated using a gradient 2-D gel. An efficient extraction/precipitation system was developed and used for the enrichment of surfactant proteins. The result of the BALF proteome analysis show the presence of several isoforms of SP-A, in which an N-non-glycosylierte form and several proline hydroxylations were identified. Furthermore, a number of protein spots were found to contain a mixture of proteins unresolved by 2-D gel electrophoresis, illustrating the feasibility of high-resolution mass spectrometry to provide identifications of proteins that remain unseparated in 2-D gels even upon extended pH gradients.