[Advantage of load-bearing osteosynthesis of pertrochanteric fractures in geriatric traumatology]. / Stellenwert einer belastungsstabilen Osteosynthese pertrochanterer Frakturen in der Gerontotraumatologie.

The problems experienced by most patients with trochanteric fractures are caused by their advanced age, particularly multimorbidity and osteoporosis, and due to this early postoperative functional treatment is only possible with full weight-bearing ability. To avoid perforation of the femoral head by overstress and collapse of the weak cancellous bone, any stabilizing device should be designed with an H-beamed blade, providing a large load-bearing surface. In our experience the 130 degrees-Double-T-blade-Plate is an effective implant for the treatment of pertrochanteric fractures, offering high stability, a large load-bearing surface, comparable complications with those known in other devices, easy and fast implantation, and low costs.

Experimental liver membrane antibodies (LMA) and antibodies against "liver specific protein (LSP)"--a comparative in vitro study.

Experimental antisera against the 26 kD rat liver protein--recently defined as a target antigen of LMA--and against "LSP" were tested on tissue sections and isolated hepatocytes from rat as well as with a variety of subcellular fractions as antigens. Anti-26 kD protein resulted in sharp immunofluorescence staining of hepatocellular plasma membranes in liver sections and on isolated hepatocytes, while the antiserum did not react with intracellular structures and was also negative with tissue sections from kidney and heart. Anti-"LSP" stained the plasma membranes of isolated hepatocytes, the cytoplasma of liver and kidney sections as well as the connective tissue of heart sections. In Western blot studies anti-26 kD protein showed a single band at 26 kD when liver plasma membranes and soluble liver protein fractions were used as antigens; a weak reaction was observed with microsomes and soluble kidney protein fractions, but there was no reaction with mitochondria or soluble heart proteins. Anti-"LSP" reacted with various proteins of the subcellular fractions between 16 and 116 kD. The 26 kD protein was found in peak II of Sepharose 6B chromatography of soluble liver protein fractions but was absent in the "LSP" fraction (peak I). We conclude that experimental LMA and anti-"LSP" recognize different epitopes of the hepatocellular plasma membrane.