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- W2070548599 abstract "Abstract. By preparative isoelectric focussing of a highly purified LH preparation in a sucrose density gradient, four biologically active LH components were isolated. The effect of neuraminidase treatment of each component on the charge heterogeneity was studied by isoelectric focussing followed by in vitro biological and immunochemical techniques. The number of biologically active components with pI-values > 7 containing varying amounts of sialic acid is at least six. The pI-value of the most basic (= asialo) LH component was 9.26. The two most basic components were not present in our preparation (NM 14) before neuraminidase treatment. It is concluded that the difference between the pI-values of LH components is caused by a difference in sialic acid content. When an intact LH component was incubated with neuraminidase there was detectable dissociation owing to the elevated temperature (37°C) and necessary acidic conditions of the incubation. Under these conditions we found the same subunits as we have described before. The most basic α-subunit had a pI-value of 9.29, whereas two β-subunits with pI > 9 were observed at pI 9.26 and pI 9.9. On the other hand, when an LH component was forced to dissociate by incubation at 56°C prior to neuraminidase digestion, two additional α-subunits were found. From this it is concluded that in the intact LH molecule, some sialic acid residues are poorer substrates for neuraminidase action than in the free subunits." @default.
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- W2070548599 date "1987-04-01" @default.
- W2070548599 modified "2023-10-14" @default.
- W2070548599 title "Heterogeneity of human luteinizing hormone. Effect of neuraminidase treatment on biologically active hormone and α- and β-subunits" @default.
- W2070548599 doi "https://doi.org/10.1530/acta.0.1140577" @default.
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