Reactions of electron-transfer proteins at electrodes.
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Biomedical subjects
Publications and source records attributed to O Hill.
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Trypsin treatment of intact cells or isolated plasmalemmae from embryonic chick neural retinae leads to an accumulation of lysophospholipids in the plasmalemmae. Trypsin was used at activities commonly used in cell disaggregation techniques. This accumulation appears to result from the decrease in acyltransferase activity in the plasmalemma produced by enzyme treatment. Plasmalemmal CoA ligase activity is not affected by trypsin treatment. Trypsinization has little effect on plasmalemmal phospholipase A2 activity. These results are discussed in relation to (a) the effects of trypsinization on cell adhesion, and (b) the theory that cells cannot adhere to lecithins because of their fluidity or surface-free-energy values. We propose that the effects of trypsinization on adhesion may in large part be due to the effects on other plasmalemmal proteins. Similarly the inability of cells to adhere to lecithin substrates is simply explained as being due to the lysolecithin that contacting cells release from these substrates.
Fifty-three cases of fractures of edentulous mandibles were reviewed and analyzed. Thirty-three cases were sufficiently documented to assess the entire treatment course. Two nonunions were identified. Major factors contributing to the difficulty of repair of fractures include the location of the fracture, the height of the horizontal ramus, and the patient's systemic condition. Closed reduction of fractures of atrophic mandibular bodies is advocated. Although anatomical alignment may not be achieved by this approach, it may preclude nonunion and a prolonged clinical course.
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