Helical Nature of the Ciliary Beat of Paramecium multimicronucleatum*

SYNOPSIS. Phase and interference cinemicrographs of cilia of Paramecium multimicronucleatum, immersed 3–24 hours in 1.0% methyl cellulose, revealed that 1) in swimming Paramecium the cilia beat with a traveling helical wave from base to tip rather than with the back and forth movement usually assumed, 2) during ciliary reversal the cilia merely change direction, but continue to beat with a traveling helical wave, and 3) in stationary Paramecium the beat is conicoidal. The traveling wave appears as an undulatory wave about 1 1/4 wave lengths long in both surface and profile views, and therefore must be helical. Envelope of the wave is cylindrical except near the base. Observations were confirmed in media without methyl cellulose by means of high speed cinemicrography, up to 4000 frames/sec. The back and forth movement, as described in all textbooks and monographs, is based mostly on 1) analogy to the abfrontal cilia (cirri) of Mytilus, which do beat with a back and forth movement, and 2) conclusions drawn from fixed preparations which do not represent what actually happens in a living animal. In a stationary Paramecium the envelope of the beat is conicoidal as seen in profile, but probably is a spiral wave, i.e., similar to a helix but increasing in diameter from base to tip. This change in wave form could be caused by the increase in resistance of the water in a stationary organism over one that is moving. Cilia and flagella (also ciliates and flagellates) are usually distinguished on the basis of wave form, but the present observations, together with previous data on flagella, show that such distinctions are untenable.     

Hierarchy of cytotoxic T cell clones. II. Intraclonal triggering of lysis by hapten-specific CTL

Cells from clones of anti-hapten murine cytotoxic T lymphocytes (CTL) can act as both target and effector cells, but will not lyse members of the same clone. The effect of haptenation on the cytolytic activity of anti-fluorescein (FL) and anti-trinitrophenol (TNP) CTL clones was examined. Treatment of anti-FL clones with fluorescein isothiocyanate or anti-TNP clones with trinitrobenzene sulphonic acid induces these clones to kill in an antigen-independent fashion. Targets killed by the haptenated CTL included syngeneic and allogeneic B lymphocyte blast cells, P815, YAC-1 and in one case human GM 4072 tumor cells. The importance of CD8 and T cell receptor (TCR) occupancy is demonstrated by the ability to block autotriggering by antibody directed against Ly 2 and the TCR. The results demonstrate that effects other than antigen recognition of the target play a role in the final outcome of effector-target cell interactions and provide a mechanism which could lead to autodestruction and immunosuppression particularly in some types of viral infection.     

Stabilization,solubilization, partial purification and some properties of cytochrome P-450 present in CaCl2-precipitated human placental microsomes

Two forms of a carbon monoxide-binding cytochrome were found to exist in CaCl₂-precipitated microsomal subfractions of human placental homogenates at term. These exhibited absorption maxima at wavelengths of 450 nm and 421–432 nm. Conversion of P-450 to the degradation product could be prevented by resuspension of the microsomes in buffered solutions containing 20% glycerol and 10^?4M dithiothreitol. Solubilization of such resuspended microsomes with sodium cholate could be effected with minimal degradation. The solubilized pigment then could be partially purified by differential fractionation with ammonium sulfate. The partially purified cytochromes did not appear to bind desmethylimpramine but did bind aniline and nicotinamide to yield atypical type II difference spectra with maxima at 435 nm and minima at 416 nm. A type I difference spectrum could be elicited with androstenedione and a spectral dissociation constant (K_S) of 4.7×10^?8M was obtained. Androstenedione also appeared to effectively prevent the binding of carbon monoxide to the cytochrome.