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Literature summary for 3.4.21.45 extracted from

  • Tsiftsoglou, S.A.; Arnold, J.N.; Roversi, P.; Crispin, M.D.; Radcliffe, C.; Lea, S.M.; Dwek, R.A.; Rudd, P.M.; Sim, R.B.
    Human complement factor I glycosylation: structural and functional characterisation of the N-linked oligosaccharides (2006), Biochim. Biophys. Acta, 1764, 1757-1766.
    View publication on PubMed
Search for more literature for 3.4.21.45

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
892
-
 Man3GlcNAc2 core, deduced molecular weight of N-linked glycan structure Homo sapiens
1622
-
 A2G2, deduced molecular weight of N-linked glycan structure Homo sapiens
1824
-
 A3G2, deduced molecular weight of N-linked glycan structure Homo sapiens
1912
-
 A2G2S1, deduced molecular weight of N-linked glycan structure Homo sapiens
2115
-
 A3G2S1, deduced molecular weight of N-linked glycan structure Homo sapiens
2202
-
 A2G2S2, deduced molecular weight of N-linked glycan structure Homo sapiens
2277
-
 A3G3S1, deduced molecular weight of N-linked glycan structure Homo sapiens
2405
-
 A3G2S2, deduced molecular weight of N-linked glycan structure Homo sapiens
2567
-
 A3G3S2, deduced molecular weight of N-linked glycan structure Homo sapiens
3569
-
 approximate reduction of molecular weight for the heavy chain after partial deglycosylation of native protein with ABS, BTG and GuH exoglycosidases Homo sapiens
5632
-
 approximate reduction of molecular weight for the light chain after partial deglycosylation of native protein with ABS, BTG and GuH exoglycosidases Homo sapiens
9201
-
 approximate reduction of molecular weight for total molecule of factor I after partial deglycosylation of native protein with ABS, BTG and GuH exoglycosidases Homo sapiens
27590
-
 calculated for non-glycosylated light chain, estimated basing upon results of the N-linked glycan analysis Homo sapiens
30270
-
 estimated for light chain of a partially deglycosylated factor I bearing a single N-linked Man3GlcNAc2 core structure at each glycosylation site Homo sapiens
35290
-
 calculated for non-glycosylated heavy chain, estimated basing upon results of the N-linked glycan analysis Homo sapiens
35900
-
 native light chain, estimated basing upon results from the N-linked glycan analysis Homo sapiens
37960
-
 estimated for heavy chain of a partially deglycosylated factor I bearing a single N-linked Man3GlcNAc2 core structure at each glycosylation site Homo sapiens
41530
-
 native heavy chain, estimated basing upon results from the N-linked glycan analysis Homo sapiens
62880
-
 total calculated molecular weight for non-glycosylated factor I, estimated basing upon results of the N-linked glycan analysis Homo sapiens
68230
-
 estimated for total protein bearing a single N-linked Man3GlcNAc2 core structure at each glycosylation site Homo sapiens
77430
-
 deduced for total protein of the native factor I basing upon results from the N-linked glycan analysis Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P05156 encoded by CFI gene
-

Purification (Commentary)

Purification (Comment) Organism
gel filtration, SDS-PAGE Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
serum
-
 Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 proteolytic activities of the native and partially deglycosylated forms analyzed, similar activities against complement component C3 indicated, charged glycans of complement factor I do not influence cofactor-substrate binding properties Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
complement component C3 + H2O structural but not functional roles for the three N-linked oligosaccharide chains indicated, N-linked glycan pool composition of the heavy and light chains indicated Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
heterodimer composed of two disulfide linked chains, each carrying three N-linked oligosaccharide chains, 25-27% N-glycosylation, 55% disialylated structures for the heavy chain and 62% disialylated structures for the light chain identified, 40% monosialylated structures for the heavy chain and 35% monosialylated structures for light chains identified, A2G2S2 identified as the dominant type of glycan on both chains, biantennary structure with chains terminating in sialic acid linked to galactose, deduced from glycan characterization Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 proteolytic assay on substrate C3(NH3) Homo sapiens