NEW ARGININE-CONTAINING PEPTIDES ISOLATED FROM CHLORELLA CELLS

Seven kinds of arginine-containing peptides were isolated fromthe cells of Chlorella ellipsoidea, and their structures wereinvestigated. Their amino acid make-ups and quantities presentin randomly grown algal cells were found to be as follows (indecreasing order of contentin moles per dry weight of cells): Arg-Arg, Arg-Arg-Glu, Arg-Arg-Arg, Arg-Glu> Arg-(Arg₂, Glu)-Glu>Arg-(Arg₃,Glu), Arg-(Glu, Asp) Using synchronously mass-cultured algal cells, the quantitiesof these peptides as they changed during the algal life cyclewere followed. It was found that, except in the case of Arg-Arg-Arg,the contents (in moles per dry weight of cells) of the peptides(i) markedly increased during the stages from D_n to L₁, (ii)remained almost constant or more or less appreciably increasedduring the stages from L₁ to L₃, and (iii) decreased sharplyduring the transformation of L₃-cells (via L₄) into D_n-cellsin the dark. The content of Arg-Arg-Arg remained almost constantduring the period from D_n to L₃, and on transference of L₃-cellsin the dark it increased temporarily and then decreased duringthe transformation of L₄-cells into D_n-cells. Significance andpossible roles of these peculiar peptides in the life cycleof Chlorella were discussed. (Received May 10, 1965; )     

Specific inhibitory effect of copper on cellular division in Chlorella

By growing Chlorella ellipsoidea synchronously by the techniqueof TAMIYA et al. with some modifications, it was demonstratedthat cellular division of ripened cells (L₂- and L₃-cells) inthe dark is specifically inhibited—especially stronglyat pH 6.3—by cupric ion present in the medium. The possibleattack site of cupric ion in cellular division of this algais discussed. (Received March 12, 1969; )     

PURIFICATION AND PROPERTIES OF THE PROTHORACICOTROPIC HORMONE OF THE SILKWORM, BOMBYX MORI

A simple and highly reproducible procedure for partial purification of prothoracicotropic hormone (PTTH) was established starting with 96,000 male adult Bombyx heads. Approximately 28,500-fold purification of PTTH was accomplished with a yield of about 50% and 6 ng of the most purified preparation ("highly purified PTTH") caused adult development in a brainless Samia pupa. The peptidal nature of PTTH was reconfirmed through the effects of various enzymatic and chemical treatments on the biological activity of "highly purified PTTH". Gel-filtration indicated the molecular weight of PTTH to be 4,400.