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R D Frankel

Publications and source records attributed to R D Frankel.

4 recordsLinked to original sources

Time-resolved x-ray diffraction study of photostimulated purple membrane.

A nanosecond resolution laser-driven x-ray source has been used to perform a time-resolved, x-ray diffraction study of the purple membrane of the Halobacterium halobium. Alterations in diffraction patterns have been observed 1 ms after photostimulation, and are interpreted to show disorder of bacteriorhodopsin packing in the plane of the membrane with little bacteriorhodopsin structural change.

Bacteriorhodopsins↗

Nanosecond X-ray diffraction from biological samples with a laser-produced plasma source.

By using 4.45-angstrom radiation generated by Cl+15 ions in a laser plasma and nanosecond exposures, low-angle x-ray diffraction patterns were obtained from dried rat spinal nerves and a powder of cholesterol. Three to four 400-picosecond, 45-joule pulses were required for the exposure. This new technique should have wide application in structural kinetic studies.

Animals↗

Identification of locally synthesized proteins in proximal stump axons of the neurotomized hypoglossal nerve.

Analysis of radioactively labeled proteins was carried out on microsamples of myelin-free axons isolated from neurotomized and normal hypoglossal nerves of the rabbit after in vitro incubation with [3H]leucine. Major radioactive peaks in axonal endings of the proximal stump 18 h after neurotomy, identified by autoradiography of microelectrophoregrams, had apparent molecular weights of 52,000d, 41,000d and 18,000d. This autoradiographic pattern differed from that of axons of untransected nerve in: (1) not having a prominent 100,000d component present in the latter; and (2) having a novel 41,000d component not present in the latter. Labeling of axonal proteins in the proximal stump in vivo resulted in no apparent retrograde transport during the 5 h studied. Autoradiographic analysis of labeled proteins released by nerves into the medium during in vitro incubation revealed a major radioactive peak with an apparent molecular weight of 77,000d. Attempts to demonstrate uptake of the 77,000d component by unlabeled axons in vitro and in vivo were unsuccessful. The hypothesis was advanced that the 52,000d protein may be neurofilament protein, and the possible significance of the 41,000d component was discussed in the contexts of the pathology of the traumatized proximal stump, and of the antecedent events leading to axonal outgrowth.

Animals↗