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PubMed · 10072639

Reference typing report for complement component C6: protein typing.

G Geserick·H Schröder·A Correns
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Abstract

Within the C6/C7/C9 Session of the VIIth Complement Genetics Workshop and Conference, various C6 protein allotypes collected from four laboratories were examined using polyacrylamide gel isoelectric focusing (PAGIF) followed by direct immunofixation. Nineteen different variants including 17 recognized allotypes and introducing two new allotypes were distinguished besides the two common allotypes C6 A and C6 B. They were designated basically according to the previous statement on C6 nomenclature. Details on C6 DNA markers and associations of C6 markers with deficiencies of terminal complement components are published in the preceding paper of this issue.

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G Geserick, H Schröder, A Correns. 1998. Reference typing report for complement component C6: protein typing.. https://doi.org/10.1159/000019083

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PubMed1991

Functional and structural domains of the sixth component (C6) of human complement.

The effects of serine protease inhibitors, diisopropyl fluorophosphate (DFP) and phenylmethanesulfonyl fluoride (PMSF), on hemolytic activity of C6 were reinvestigated. C6 was inactivated in a range of 1-10 mM by both of the inhibitors as previously reported. Limited proteolytic digestion was also studied to elucidate the functional and structural domains of C6. The major fragments produced by trypsin, plasmin, or lysyl endopeptidase could not be separated unless disulfide bonds were disrupted, but Staphylococcus aureus V8 protease yielded several fragments, each of which was not linked by disulfide bond. When C6 labeled with [3H]DFP was subjected to limited digestion with V8 protease, a fragment with a molecular weight of 38 kilodaltons (kDa) was mainly labeled and other fragments of 53 kDa and 26.4 kDa were also faintly labeled, while fragment 35 kDa wasn't labeled, indicating specific domains reactive with DFP. On the other hand, when C6 with or without DFP treatment was digested with V8 protease and those fragments were incubated with C5 and subjected to sucrose density ultracentrifugation, fragments 53, 38, 35 and 27.5 kDa interacted with C5 in both cases. These results suggest that C6 modified by DFP can interact with C5, and the amino-terminal sequences of fragment 38 and 35 kDa suggest the binding domain of C6 with C5 takes place within the two short consensus repeats.

Complement C6↗
PubMed1990

C6 reference typing report.

Various C6 protein allotypes were examined using polyacrylamide gel isoelectric focusing followed by immunoblotting or hemolytic overlay. For several 'difficult' allotypes, neuraminidase treatment of samples and long-distance isoelectric focusing gels were applied. Nineteen different allotypes were distinguished besides the two common allotypes C6 A and C6 B. They were designated basically according to the previous statement on C6 nomenclature [Mauff et al., 1980].

Complement C6↗