ABSTRACT
Polybutester is a unique copolymer that can be extruded as a flexible monofilament nonabsorbable suture. The mechanical performance of this new suture material was compared with that of polypropylene and nylon. The results indicate that polybutester sutures are as strong, have the same degree of total elongation at break and knot as the other monofilament sutures. In contrast with polypropylene and nylon sutures, the polybutester sutures have a perceptible stretch, are more elastic and flexible, and exhibit less creep. Polybutester sutures appear to be an acceptable alternative to polypropylene and nylon sutures and their unique mechanical properties may even prove to be superior in vivo.
Subject(s)
Polyesters/standards , Sutures/standards , Elasticity , Nylons/standards , Polypropylenes/standards , Suture Techniques , Tensile StrengthSubject(s)
Needles , Biomedical Engineering , Evaluation Studies as Topic , Rotation , Stress, MechanicalABSTRACT
Antisera specific for the basic peroxidase from horseradish (Amoracea rusticana) were used to examine homology among horseradish peroxidase isoenzymes and among basic peroxidases from root plants. The antisera cross-reacted with all tested isoperoxidases when measured by both agar diffusion and quantitative precipitin reactions. Precipitin analyses provided quantitative measurements of homology among these plant peroxidases. The basic radish (Raphanus sativus L. cv. Cherry Belle) peroxidase had a high degree of homology (73 to 81%) with the basic peroxidase from horseradish. Turnip (Brassica rapa L. cv. Purple White Top Globe) and carrot (Daucus carota L. cv. Danvers) basic peroxidases showed less cross-reaction (49 to 54% and 41 to 46%, respectively). However, the cross-reactions of antisera with basic peroxidases from different plants were greater than were those observed with acidic horseradish isoenzymes (30 to 35%). These experiments suggest that basic peroxidase isoenzymes are strongly conserved during evolution and may indicate that the basic peroxidases catalyze reactions involved in specialized cellular functions. Anticatalytic assays were poor indicators of homology. Even though homology among isoperoxidases was detected by other immunological methods, antibodies inhibited only the catalytic activity of the basic peroxidase from radish.
