Three mice and one rabbit were inoculated with purified human fibroblastoid interferon. Neutralizing activity to human fibroblastoid interferon was observed in the serum of these animals with the rabbit showing the highest anti-interferon titers (10(6) neutralizing units/mL). Rabbit antiserum was coupled to cyanogen bromide activated Sepharose, and the resulting material was tested for use in the purification of human fibroblastoid interferon. Pure interferon obtained by this procedure was analyzed, and we report the sequence of the first 13 N-terminal amino acid residues of this protein.
The effect of chloramphenicol (CAP) on cell division and organelle ultrastructure was studied during light-induced chloroplast development in the Chrysophyte alga, Ochromonas danica . Since the growth rate of the CAP-treated cells is the same as that of the control cells for the first 12 hr in the light, CAP is presumed to be acting during that interval solely by inhibiting protein synthesis on chloroplast and mitochondrial ribosomes . CAP markedly inhibits chloroplast growth and differentiation . During the first 12 hr in the light, chlorophyll synthesis is inhibited by 93 17 /c , the formation of new thylakoid membranes is reduced by 91 7 0, and the synthesis of chloroplast ribosomes is inhibited by 81 % . Other chloroplastassociated abnormalities which occur during the first 12 hr and become more pronounced with extended CAP treatment are the presence of prolamellar bodies and of abnormal stacks of thylakoids, the proliferation of the perinuclear reticulum, and the accumulation of dense granular material between the chloroplast envelope and the chloroplast endoplasmic reticulum . CAP also causes a progressive loss of the mitochondrial cristae, which is paralleled by a decline in the growth rate of the cells, but it has no effect on the synthesis of mitochondrial ribosomes . We postulate that one or more chloroplast ribosomal proteins are synthesized on chloroplast ribosomes, whereas mitochondrial ribosomal proteins are synthesized on cytoplasmic ribosomes .
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