Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UNIPROT:P00790 (
PGA
)
2,475
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The action of six different enzymes on the function and structure of
Factor H
was investigated by use of sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, haemagglutination, two enzyme-linked immunosorbent assay systems and an assay for Factor I cofactor activity. Six monoclonal antibodies directed against the 38 kDa tryptic fragment of
Factor H
[which contains the binding site for C3b (a 180 kDa fragment of the third component of complement) and the cofactor activity] were also used to detect cleavage products derived from the same fragment. Elastase, chymotrypsin A4 or trypsin first cleaved
Factor H
to 36-38 kDa fragments carrying all six monoclonal anti-(
Factor H
)-binding sites. In parallel, the interaction of
Factor H
with surface-bound C3b was lost, whereas the cofactor function was preserved. Further cleavage of the 36-38 kDa fragments into two 13-19 kDa fragments (one carrying the MAH4 and MRC OX 24 epitopes, the other the MAH1, MAH2, MAH3 and MRC OX 23 epitopes) destroyed cofactor activity.
Pepsin
, bromelain or papain rapidly split off a 13-15 kDa fragment of
Factor H
carrying the MAH1, MAH2, MAH3 and MRC OX 23 epitopes and destroyed all tested functions of
Factor H
. Ficin cleaved
Factor H
into disulphide-linked fragments smaller than 25 kDa, but did not affect the functions of the
Factor H
molecule. The 38 kDa tryptic fragment of
Factor H
is the N-terminal end of the
Factor H
molecule, as determined by N-terminal sequence analysis. A model is presented of the substructure of
Factor H
.
...
PMID:Structural and functional analysis of the complement component factor H with the use of different enzymes and monoclonal antibodies to factor H. 293 33
