By J. Vincent Edwards and Tyrone L. Vigo (Eds.)
content material: Biologically lively fibers in overall healthiness care / J. Vincent Edwards and Tyrone L. Vigo --
Retention, unfolding, and deformation of soluble proteins on solids / S.C. Goheen ... [et al.] --
a unique, enzyme-based strategy for the wound-surface removing and decontamination of organophosphorus nerve brokers / Janet ok. Grimsley ... [et al.] --
figuring out dressing composition : a biomaterial standpoint / George P. Hansen --
The non-healing wound : mechanisms and dressings / Dorne R. Yager ... [et al.] --
layout, training, and task of cotton gauze to be used in power wound study / J. Vincent Edwards ... [et al.] --
A hybrid bioabsorbable wound dressing / A. London Brown ... [et al.] --
Carboxymethylation-cotton for wound care administration / D.V. Parikh --
Arterial grafts as biomedical textiles / Martin Bide ... [et al.] --
Biologically lively biodegradable biomaterials / C.C. Chu --
Antimicrobial polymers and fibers : retrospective and potential / Tyrone L. Vigo --
settling on antimicrobial efficacy and biocompatibility of taken care of articles utilizing commonplace try tools / Beth Gresham Joiner --
Antimicrobials for man made fibers / Walter Bender and Peter Stutte --Durable and regenerable antimicrobial textiles / Gang solar --
Antimicrobial homes of a unique N-halamine-based cellulose therapy procedure / Jeffrey Williams ... [et al.] --
Biodeterioration of wool via microorganisms and bugs / Jeanette M. Cardamone.
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Elastase binds to the peptide Val-Pro-Val and it was anticipated that this peptide would sequester elastase if the peptide was bound to cotton. We attached Val-ProVal to cotton so that either the carboxy terminal or amino terminal end would be exposed to the solution. In testing these two peptides, the COO-terminal peptide bound more elastase than the N H 2 terminal form. Finding the correct orientation of the Val-Pro-Val peptide on the solid may help elucidate the biochemical process by which the inhibitory Val-Pro-Val sequence binds and reduces elastase activity.
This has prompted considerable research into the immobilization of Ο Ρ Η onto several solid supports to be used as solid-phase, flow-through reactors for nerve agent detoxification and disposal. These supports include nylon, trityl agarose, and polyurethane (21-24). The enzyme has also been successively cross-linked into polyurethane sponges and foams for nerve agent cleanup on structural surfaces (2527). The present work describes the preparation of cotton towelettes to which both the wild type and the H254R/H257L enzyme have been covalently bound.
During our studies of cytochrome c, we observed that unfolding on a surface occurred at a lower temperature than it does in solution. We were not able to determine whether the conformational change on the sorbent was the same as it was in solution at a slightly higher temperature. However, there was a lowering of the kinetic energy requirement for unfolding to occur. We can express this relationship graphically in Figure 6, where both the activation energy and the energy of the product are lowered by the presence of a surface.
Bioactive Fibers and Polymers by J. Vincent Edwards and Tyrone L. Vigo (Eds.)