Interaction of rabbit secretory component with rabbit IgA dimer.

Details

Serval ID
serval:BIB_1939CD34428E
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Interaction of rabbit secretory component with rabbit IgA dimer.
Journal
Journal of Biological Chemistry
Author(s)
Kühn L.C., Kraehenbuhl J.P.
ISSN
0021-9258
Publication state
Published
Issued date
11/1979
Peer-reviewed
Oui
Volume
254
Number
21
Pages
11066-11071
Language
english
Abstract
Secretory component (SC), a glycoprotein with an apparent molecular weight of approximately 80,000, has been isolated from rabbit milk and found to be heterogenous in size and charge. Functionally intact IgA dimer has been dissociated from milk secretory IgA using a chaotropic agent and further purified to homogeneity. The interaction between SC and IgA dimer is a reversible time- and temperature-dependent process. At 23 degrees C, the association rate constant (2.4 x 10(5) M-1 min-1) and the dissociation rate constant (1.8 x 10(-3) min-1) have been measured independently and the affinity constant based on these rates (1.3 x 10(8) M-1) is similar to that calculated from Scatchard plots (1.9 x 10(8) M-1). One class of binding sites has been estimated from Scatchard plots in spite of the observed heterogeneity of SC. The interaction is tighter at low temperatures because the decrease in dissociation rate is greater than the decrease in association rate. The thermodynamic calculations reveal a delta G of -11.0 kcal . mol-1, a delta H of -8.9 kcal . mol-1 and a delta S of +7.0 cal. mol-1 degree-1. The pH range over which interaction occurs is rather large (5 to 8) with no significant differences in apparent Ka.
Keywords
Animals, Female, Glycoproteins, Immunodiffusion, Immunoglobulin A/isolation & purification, Immunoglobulin Fragments/isolation & purification, Kinetics, Macromolecular Substances, Milk/immunology, Molecular Weight, Pregnancy, Protein Binding, Rabbits, Rats, Secretory Component/isolation & purification
Pubmed
Web of science
Create date
25/01/2008 15:06
Last modification date
20/08/2019 12:49
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