:Differences in the affinity to 5'-AMP-Sepharose 4B

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In this report, we described the differences of immunoglobulin-linked LDH in affinity to 5'-AMP-Sepharose 4B by use of the mini-column method and discussed them with respect to the kinetic properties.Affinity of immunoglobulin-linked LDH whose electropherograms exhibited broad patterns (broad pattern type) was different from that of immunoglobulin-linked LDH with extra bands in enzymograms (extra band type).In the cases of extra-band types due to either IgA- or IgG-linkage, LDH activities were not detected in the unadsorbed fractions and completely recovered in the NADH fractions of 5'-AMP-Sepharose 4B. Recovery of LDH activities derived from immunoglobulin-linked LDH was also confirmed by high speed liquid chromatography. On the other hand, in the cases of broad pattern types of IgG-linked LDH, LDH activities and those derived from IgG-linked LDH were eluted in the both two fractions.IgA-linked LDH (extra band) could not be distinguished from normal sized LDH in their Km values for β-NADH, Km values of IgG-linked LDH (broad pattern) were observed slightly larger than those of normal sized LDH. Ki values of IgA-linked LDH (extra band) for 5'-AMP against β-NADH were intermediate between those of LDH-1 and LDH-5.These results indicated that broad pattern types of IgG-linked LDH would have lower affinity to 5'-AMP-Sepharose 4B than extra-band types of immunoglobulin-linked LDH and normal sized LDH.
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