Le rôle des créanciers et des institutions financières dans la survie des entreprises en difficulté en droit belge

In the first part of this article, Me Foriers explains the Belgium Laws on collective procedures and the peculiar and interesting efforts of the Bankruptcy Courts to detect the legal signals of a failing enterprise while it is still possible to avoid bankruptcy as well as the means used to redress the situation. In the second part, the author discusses the professional liability of the banking institution when a line of credit is granted or refused to an ailing enterprise. On this last aspect, Belgium Law is similar to French Law discussed in Professor's Gavalda article

Binding of hydrophobic ligands to plant lectins: Titration with arylaminonaphthalenesulfonates

Binding of the Hydrophobic ligands 1,8-anilinonaphthalenesulfonic acid (ANS) and 2,6-toluidinylnaphthalenesulfonic acid (TNS) to a variety of plant lectins was studied by lectin-induced alteration of the fluorescence spectra of the two ligands. With one exception, all legume lectins examined bound ANS, with affinity constants ranging from 103 to 104 M-1. Similar ANS binding was noted for some nonlegume lectins. Titration of the five isolectins from Phaseolus vulgaris with ANS indicated positive cooperative binding of ANS to the two isolectins E4 and E3L1. Titrations with TNS revealed high-affinity sites for this ligand in a number of lectins. Addition of haptenic sugars did not inhibit binding of ANS, suggesting that the hydrophobic binding sites of lectins are independent of the carbohydrate binding sites.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/25163/1/0000599.pd

A structural comparison of the A and B subunits of Griffonia simplicifolia I isolectins

A structural comparison between the A and B subunits of the five tetrameric Griffonia simplicifolia I isolectins (A4, A3B, A2B2, AB3, B4) was undertaken to determine the extent of homology between the subunits. The first 25 N-terminal amino acids of both A and B subunits were determined following the enzymatic removal of N-terminal pyroglutamate blocking groups with pyroglutamate aminopeptidase. Although 21 amino acids were common to both subunits, there were four unique amino acids in the N-terminal sequence of A and B. Residues 8, 9, 17, and 19 were asparagine, leucine, lysine, and asparagine in subunit A and threonine, phenylalanine, glutamic acid, and serine in subunit B. The last six C-terminal amino acids, released by digestion with carboxypeptidase Y, were the same for both subunits: Arg---(Phe, Val)---Leu---Thr---Ser---COOH. Subunit B, which contains one methionyl residue, was cleaved by cyanogen bromide into two fragments, a large (Mr = 31,000) and a small (Mr = 2700) polypeptide. Failure of the small fragment to undergo manual Edman degradation indicated an N-terminal blocking group, presumably pyroglutamate. Both subunits were digested with trypsin and the tryptic peptides were analyzed using reverse-phase HPLC. Tryptic glycopeptides were identified by labeling the carbohydrate moiety of the A and B subunit using sodium [3H] borohydride. Cysteine-containing tryptic peptides were similarly identified by using [1-14C]iodoacetamide. Approximately 30% of the tryptic peptides were common to both subunits. Thus, although the N- and C-terminal regions of A and B are similar, the subunits each possess unique sequences.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/24903/1/0000330.pd

Leveraged Corporate Control : Zijn er lessen te trekken uit de Amerikaanse ‘Dual-Class Share’ en ‘Tenure Voting’ structuren voor het Belgische loyauteitsstemrecht ?

status: publishe

L'état des recherches de logique juridique en Belgique

info:eu-repo/semantics/publishe

Allocution de Monsieur Paul Foriers

info:eu-repo/semantics/publishe

La motivation par référence à la nature des choses

info:eu-repo/semantics/publishe