The binding of human milk lactoferrin to immunoglobulin A |
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Authors: | T Watanabe H Nagura K Watanabe W R Brown |
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Affiliation: | 1. Cell Biology Research Laboratory, Tokai University School of Medicine, Isehara, Kanagawa 259-11, Japan;2. Department of Pathology, Tokai University School of Medicine, Isehara, Kanagawa 259-11, Japan;3. Department of Medicine, University of Colorado, Health Science Center and VA Hospital, Boulder, CO 80302, USA |
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Abstract: | To define the step at which translational initiation factor IF1 exercises its stimulation, initial rate kinetic analyses of 30 S initiation complex formation were carried out in the presence and absence of this factor. It was shown that, without affecting the affinity of the ribosomes either for the initiator tRNA or for the poly(AUG) used as template, IF1 increases approximately 2.5-fold the limiting Vmax of the 'pre-ternary complex'----ternary complex transition which represents the rate-limiting step in 30 S initiation complex formation. This kinetic effect titrates with the 30 S ribosomal subunit which must therefore represent the target of IF1 action. |
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Keywords: | Lactoferrin Secretory IgA Secretory component IgA affinity column LF, lactoferrin sIgA, secretory IgA SC, secretory component PAGE, polyacrylamide gel electrophoresis |
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