ABSTRACT
In contrast with autographic or allographic repair materials, the use of a xenographic soft tissue repair material could improve patient outcomes following surgery, since such a material would not require a second surgical site and could reduce the risk of human-to-human disease transmission. Veritas(c) Collagen Matrix (Veritas) is a novel, non-crosslinked soft tissue repair material derived from bovine pericardium. Physical property testing shows this material is strong, malleable, of uniform thickness, and easily sutureable. Biocompatibility testing, as well as viral safety and extractable deoxyribonucleic acid (DNA) studies demonstrate the acellularity, safety, and immunological inertness of the material. Animal studies in pigs and rabbits, in a variety of surgical procedures that include abdominal wall implant, unilateral hysterectomy, urethral sling implant, and dural substitute studies demonstrate Veritas does not adhere readily to tissues of the chest wall or abdomen under conditions that promote adhesions. In addition, these studies show that Veritas is remodelable and, in time, becomes histologically indistinguishable from the host tissue. These findings indicate Veritas is an ideal soft tissue repair material and it may serve as an ideal scaffold for tissue engineering.
Subject(s)
Biocompatible Materials/chemistry , Epoxy Compounds/chemistry , Pericardium/chemistry , Tissue Engineering/instrumentation , Tissue Engineering/trends , Tissue Scaffolds/trends , Animals , Cattle , Equipment Design , Equipment Failure AnalysisABSTRACT
Glyoxalase II (S2-hydroxyacylglutatione hydrolase, EC 3.1.2.6) was purified from Swiss mouse liver to homogeneity by a rapid, two-step affinity chromatographic scheme. Homogeneity was established by multiple electrophoretic determinations. The purified enzyme exhibited a specific activity of 920 I.U./mg protein and has a molecular weight of approx. 29 500 as estimated by SDS polyacrylamide gel electrophoresis. The enzyme is a basic protein with a pI of approx. 8.1. Mouse liver glyoxalase II is competitively inhibited by the substrate of glyoxalase I (the hemimercaptal of methylglyoxal and glutathione); the Ki is 0.3 mM. The Km for S-D-lactoylglutathione is 0.27 mM, and the enzyme has a turnover number of approx. 27 000 mumol substrate per min per mumol enzyme.
Subject(s)
Liver/enzymology , Thiolester Hydrolases/isolation & purification , Animals , Chromatography, Affinity , Glutathione/analogs & derivatives , Kinetics , Mice , Molecular Weight , Thiolester Hydrolases/metabolismABSTRACT
Glyoxalase I (S-lactoyl-glutathione methylglyoxal-lyase (isomerizing), EC 4.4.1.5) was purified from Swiss mouse liver to homogeneity by a rapid, two-step procedure involving hydrophobic and affinity chromatography. Homogeneity was established by multiple electrophoretic determinations and by sedimentation equilibrium centrifugation. The purified enzyme exhibited a specific activity of 944 I.U./mg protein an has a molecular weight of 43 000. The enzyme was shown to be a dimer by sodium dodecyl sulfate disc gel electrophoresis and is apparently composed of identical subunits of molecular weights approximating 21 500.