Third component of human complement: Localization of the internal thiolester bond

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چکیده

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Third component of human complement: localization of the internal thiolester bond.

Human complement protein C3 was inactivated by using methylamine and thereby generating a SH group from the internal thiol ester. The protein was coupled via this SH group to activated thiol-Sepharose and digested with elastase. Fragment C3d remained attached to the thiol-Sepharose and was subsequently eluted with L-cysteine. Concomitantly, the original SH group was regenerated, and it was then...

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Sequence determination of the thiolester site of the fourth component of human complement.

The fourth component of complement (C4) is inactivated by treatment with methylamine. This property is shared wit the third component (C3) and with alpha 2-macroglobulin. In each instance, the reaction with methylamine is stoichiometric, covalent, and accompanied by the appearance of a thiol group. These data are consistent with the presence of an internal thiolester bond. Incubation of C4 with...

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Source/Description A cDNA fragment, pC3.11 (1) was used as probe. Polymorphisms: EcoRI cleavage of genomic DNA reveals a 2 allele polymorphism with band sizes of 5.2 and 5.6 kb. Invariant bands of 11.5, 11.0, 9.0 and 3 0 kb were also present. Frequency: Estimated from 35 unrelated Caucasians. Allele Frequency Dl 5.2 0.67 D2 5.6 0.33 Chromosomal Localisation: The human C3 gene had been assigned ...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 1982

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.79.4.1054