Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Properdin”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,603 records · Page 89Linked to original sources
PubMedDate not supplied

Phylogeny of the third component of complement, C3: analysis of the conservation of human CR1, CR2, H, and B binding sites, concanavalin A binding sites, and thiolester bond in the C3 from different species.

The third component of complement, C3, binds to several other complement proteins. To study the diverse reactivities of C3, we analyzed the conservation of structural and functional features in the C3 from different species. First, we developed a method to purify swine (Po), rabbit (Rb), mouse (Mo), cobra (Co), Xenopus (Xe), axolotl (Ax), and trout (Tr) C3 from plasma. This involved protein precipitation by polyethylene glycol, followed by anion-exchange, gel filtration, and cation exchange chromatography. All C3's tested were comprised of two chains (alpha/beta-chain) and contain a thiolester bond within the alpha-chain. The two N-linked high-mannose carbohydrates found in human C3 were only conserved (as detected by ConA binding) in Rb C3. In contrast, Xe, Ax, and Tr C3 have this moiety only in the beta-chain and Po and Mo C3 only in the alpha-chain. Co C3, in contrast to cobra venom factor (CVF), lacks ConA binding carbohydrates in both chains. N-terminal amino acid sequence analysis of the alpha-, alpha'-, and beta-chains showed varying degrees of similarity within the different C3's. The N-termini of the Xe and Ax C3 beta-chains were found to be blocked. The conservation of binding sites in the different C3's for human complement receptors type one (CR1) and two (CR2) and for factors H and B was investigated due to the structural and functional similarities of these molecules and to the ability of some of them to bind to the same domain(s) in human C3.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗
PubMed1994

Convergent evolution: the need to be explicit.

Convergence as a phenomenon in molecular evolution is an issue that confuses many discussions. Often the problem is that not enough care is taken to state exactly what kind of convergence one has in mind. Functional and mechanistic convergence are both common, and some structural convergence has probably occurred, but a convincing case for genuine sequence convergence has yet to be made.

Amino Acid Sequence↗
PubMed1976

Interaction of E. coli strains with human serum: lack of relationship to K1 antigen.

Twenty-eight strains of E. coli isolated from infants were compared with respect to opsonic requirements, sensitivity to serum, and ability to activate serum chemotactic factors. Six of the strains were isolated from stools of healthy newborn infants; 22 were isolated from the cerebrospinal fluid or blood of infants with meningitis and/or septicemia. Eighteen of the strains had K1 polysaccharide antigen. Fourteen of the strains (seven with K1 antigen) activated complement via the alternative pathway and all of these strains were well opsonized in 4% pooled human serum. A higher concentration of serum was necessary to opsonize 12 of the 14 strains that did not activate the alternative pathway. A wide variation was also found in opsonic requirements of E. coli strains isolated from healthy and sick infants. There was no relationship of the K1 antigen to opsonic requirements, to capacity to activate complement via the alternative pathway, to generation of chemotactic factors, or to sensitivity to serum cidal activity. Therefore, the association of E. coli with K1 antigen and neonatal meningitis did not appear to be related to these bacteria-serum interactions.

Antigens, Bacterial↗