[Postoperative autologous transfusion in primary hip arthroplasties]. / Postoperativ autotransfusjon ved innsetting av primaere totalproteser i hoften.

100 patients who underwent primary, total hip arthroplasty were consecutively included in this study. Their postoperative sanguineous wound drainage was reinfused, and the purpose of the study was to evaluate if such reinfusion reduced the use of homologous blood. 100 patients who were operated immediately prior to the reinfusion group were used as a historical control group. The mean volume reinfused was 426 milliliters. The mean haemoglobin of the wound drainage was 7.3 g/100 ml. There was no statistically significant reduction in the use of homologous blood. Nor was there any reduction in the number of patients exposed to such blood. Autotransfusion of postoperative sanguineous wound drainage does not seem to be indicated as a routine procedure in primary total hip arthroplasties.

Isolation, ultrastructure, and partial characterization of collagen from the perineurium of the Florida lobster, Panulirus argus.

Highly concentrated extracellular filaments in the perineurium of the Florida spiny lobster, Panulirus argus, were isolated using ultracentrifugation and linear sucrose gradients. The pellet obtained was highly enriched for the filaments as observed by transmission electron microscopy. Fibril diameter and axial periodicity measurements were obtained from filaments positively and negatively stained with uranyl acetate. A period between 14.0 and 25.0 nm and an average fibril diameter of 15.0 nm were observed. The filaments proved resistant to solubilization by most conventional agents and by several collagenases. NaOH (0.1 M at 100 degrees C) safely dissolved the filaments for measurements of protein content by the Lowry method and carbohydrate content with anthrone reagent. These tests revealed a protein content of approximately 84% and a high carbohydrate content of approximately 15%. Polyacrylamide electrophoresis of an acid-pepsin filament extract revealed a highly concentrated band (approximately 100,000) corresponding to the alpha-1 and alpha-2 bands of vertebrate type I collagen. Wide angle X-ray diffraction yielded meridional reflections that confirmed the filaments as collagen when compared with mammalian collagen X-ray diffraction. The amino acid composition was determined with a computer-assisted Beckman amino acid analyzer, which showed a glycine content of 279 residues/1000. Hydroxylysine and hydroxyproline were present in lower concentrations than expected.