Chemokinesis by tetrahymena in response to bacterial oligopeptides.
The ciliate Tetrahymena responds very efficiently by chemoattraction to a group of trichloroacetic acid-soluble oligopeptides isolated from a commercial bioprotein from Methanococcus. When fractionated by reversed phase C18-high-pressure liquid chromatography, this group of very efficient chemoattractants turned out to consist of a heterogeneous group of oligopeptides with molecular weight ranging from 0.2 to 1.5 kDa. The peptides were very rich in the following amino acids: aspartic acid, alanine, glutamic acid, proline, glycine, lysine, and arginine. The term chemokinesis is used throughout to emphasise that chemoattraction does not necessarily include an element of orientation of cells.
Leick
Vagn
V
Department B, Institute of Medical Biochemistry and Genetics, The University of Copenhagen, The Panum Institute, Blegdamsvej 3C, DK-2200 Copenhagen N, Denmark. vagn@leick.dk
Lindemose
Søren
S
D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry; D002630:Chemotactic Factors / Q000737:chemistry / Q000302:isolation & purification; D002633:Chemotaxis; D017017:Methanococcus / Q000737:chemistry*; D008970:Molecular Weight; D009842:Oligopeptides / Q000737:chemistry / Q000302:isolation & purification; D016808:Tetrahymena thermophila / Q000502:physiology*
D001426:Bacterial Proteins; D002630:Chemotactic Factors; D009842:Oligopeptides