title: Biochemical aspects of neutrophil chemotaxis.
abstract: Solutions of crude casein contain a chemotactic peptide with a molecular weight of 2 200 daltons. As in the case of other cytotaxins, this compound displays hydrophobic properties. Partially purified casein cytotaxin stimulated the disproportionate oxidation of glucose-1-carbon, from which we infer that hexose monophosphate shunt activity is increased in cells exposed to cytotaxin. No evidence could be found to support the suggestion that cytotaxin stimulation leads to activation of latent cellular esterases.
mesh_terms: D000818:Animals; D002364:Caseins / Q000032:analysis; D002630:Chemotactic Factors / Q000302:isolation & purification / Q000502:physiology; D002634:Chemotaxis, Leukocyte; D004734:Energy Metabolism; D004789:Enzyme Activation; D004950:Esterases / Q000378:metabolism; D007531:Isoflurophate / Q000502:physiology; D009504:Neutrophils / Q000201:enzymology / Q000502:physiology; D010100:Oxygen / Q000097:blood; D010455:Peptides / Q000032:analysis; D011817:Rabbits
chemical_list: D002364:Caseins; D002630:Chemotactic Factors; D010455:Peptides; D007531:Isoflurophate; D004950:Esterases; D010100:Oxygen