scholarly journals CNBr cleavage of the light chain of human complement factor I and alignment of the fragments

1986 ◽  
Vol 233 (2) ◽  
pp. 339-345 ◽  
Author(s):  
J M Yuan ◽  
L M Hsiung ◽  
J Gagnon
Keyword(s):  
Sequence Analysis ◽  
Light Chain ◽  
Gel Filtration ◽  
Gel Permeation Chromatography ◽  
Complement Factor ◽  
Human Complement ◽  
Factor I ◽  
Complement Factor I ◽  
Arginine Residues ◽  
Cnbr Cleavage

The light chain and heavy chain of reduced and alkylated human complement Factor I were purified by high-pressure gel-permeation chromatography. CNBr cleavage of Factor I light chain yielded four major fragments, which were purified by gel filtration. N-Terminal sequence analysis of the CNBr-cleavage fragments allowed identification of 200 of the approx. 240 amino acid residues of the light chain. An alignment is proposed, based on sequence analysis of peptides obtained after cleavage at arginine residues of the light chain and on homology of the sequence determined with that of other serine proteinases. The sequence around the active-site serine residue was established and three potential attachment sites for carbohydrate moieties were identified.

Activity studies on human complement factor I (FI)

2002 ◽  
Vol 30 (5) ◽  
pp. A118-A118
Author(s):  
X.H. Chen ◽  
S.A. Tsiftsoglou ◽  
P.Y. Li ◽  
D.A. Mitchell ◽  
S. Salamanca ◽  
...  
Keyword(s):  
Complement Factor ◽  
Human Complement ◽  
Factor I ◽  
Complement Factor I

scholarly journals The catalytic chain of human complement subcomponent C1. Purification and N-terminal amino acid sequences of the major cyanogen bromide-cleavage fragments

1982 ◽  
Vol 201 (1) ◽  
pp. 49-59 ◽  
Author(s):  
G J Arlaud ◽  
J Gagnon ◽  
R R Porter
Keyword(s):  
High Pressure ◽  
Amino Acid ◽  
Gel Filtration ◽  
Gel Permeation Chromatography ◽  
Reversed Phase ◽  
Amino Acid Sequences ◽  
Serine Proteinases ◽  
Human Complement ◽  
Terminal Sequence ◽  
Cnbr Cleavage

1. The a- and b-chains of reduced and alkylated human complement subcomponent C1r were separated by high-pressure gel-permeation chromatography and isolated in good yield and in pure form. 2. CNBr cleavage of C1r b-chain yielded eight major peptides, which were purified by gel filtration and high-pressure reversed-phase chromatography. As determined from the sum of their amino acid compositions, these peptides accounted for a minimum molecular weight of 28 000, close to the value 29 100 calculated from the whole b-chain. 3. N-Terminal sequence determinations of C1r b-chain and its CNBr-cleavage peptides allowed the identification of about two-thirds of the amino acids of C1r b-chain. From our results, and on the basis of homology with other serine proteinases, an alignment of the eight CNBr-cleavage peptides from C1r b-chain is proposed. 4. The residues forming the ‘charge-relay’ system of the active site of serine proteinases (His-57, Asp-102 and Ser-195 in the chymotrypsinogen numbering) are found in the corresponding regions of C1r b-chain, and the amino acid sequence around these residues has been determined. 5. The N-terminal sequence of C1r b-chain has been extended to residue 60 and reveals that C1r b-chain lacks the ‘histidine loop’, a disulphide bond that is present in all other known serine proteinases.

Deficiency of Human Complement Factor I Associated with Lowered Factor H

2000 ◽  
Vol 96 (2) ◽  
pp. 162-167 ◽  
Author(s):  
G.M. Naked ◽  
M.P.C. Florido ◽  
P. Ferreira de Paula ◽  
A.M. Vinet ◽  
J.S. Inostroza ◽  
...  
Keyword(s):  
Factor H ◽  
Complement Factor ◽  
Human Complement ◽  
Factor I ◽  
Complement Factor I

Human complement factor I glycosylation: Structural and functional characterisation of the N-linked oligosaccharides

2006 ◽  
Vol 1764 (11) ◽  
pp. 1757-1766 ◽  
Author(s):  
Stefanos A. Tsiftsoglou ◽  
James N. Arnold ◽  
Pietro Roversi ◽  
Max D. Crispin ◽  
Catherine Radcliffe ◽  
...  
Keyword(s):  
Complement Factor ◽  
Human Complement ◽  
Factor I ◽  
Complement Factor I ◽  
Functional Characterisation

Cloning and characterization of the promoter for the human complement factor I (C3b/C4b inactivator) gene

Gene ◽  
1998 ◽  
Vol 208 (1) ◽  
pp. 17-24 ◽  
Author(s):  
J.O. Minta ◽  
May Fung ◽  
Stephen Turner ◽  
R. Eren ◽  
L. Zemach ◽  
...  
Keyword(s):  
Complement Factor ◽  
Human Complement ◽  
Factor I ◽  
Complement Factor I

Mapping of the human complement factor I gene to 4q25

Genomics ◽  
1989 ◽  
Vol 4 (1) ◽  
pp. 82-86 ◽  
Author(s):  
Rita Shiang ◽  
Jeffrey C. Murray ◽  
Cynthia C. Morton ◽  
Kenneth H. Buetow ◽  
John J. Wasmuth ◽  
...  
Keyword(s):  
Complement Factor ◽  
Human Complement ◽  
Factor I ◽  
Complement Factor I ◽  
I Gene

scholarly journals Tetartohedral twinning could happen to you too

2012 ◽  
Vol 68 (4) ◽  
pp. 418-424 ◽  
Author(s):  
Pietro Roversi ◽  
Eric Blanc ◽  
Steven Johnson ◽  
Susan Mary Lea
Keyword(s):  
Structure Determination ◽  
Complement Factor ◽  
Human Complement ◽  
Factor I ◽  
Complement Factor I ◽  
Rotational Part ◽  
Crystal Twinning

Tetartohedral crystal twinning is discussed as a particular case of (pseudo)merohedral twinning when the number of twinned domains is four. Tetartohedrally twinned crystals often possess pseudosymmetry, with the rotational part of the pseudosymmetry operators coinciding with the twinning operators. Tetartohedrally twinned structures from the literature are reviewed and the recent structure determination of tetartohedrally twinned triclinic crystals of human complement factor I is discussed.

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