التفاصيل البيبلوغرافية
| العنوان: |
Human complement component C1‾s. |
| المؤلفون: |
Spycher, Stefan E., Nick, Hanspeter, Rickli, Egon E. |
| المصدر: |
European Journal of Biochemistry; 4/1/86, Vol. 156 Issue 1, p49-57, 9p |
| مصطلحات موضوعية: |
CHROMATOGRAPHIC analysis, AMINO acids, HOMOLOGY (Biology), IMMUNOGLOBULIN G, GEL permeation chromatography, ION exchange (Chemistry) |
| مستخلص: |
Human Cls proenzyme (Mr 83000) was isolated by a rapid two-stage method involving affinity chromatography of Cl on IgG-Sepharose and isolation of subcomponent Cls by ion-exchange chromatography On DEA&Sephacel. Single-chain Cls proenzyme was activated to two-chain Cls with self-activated Cir. After reduction and S-carboxaxnidomethylation the heavy chain of Cls (M, 57000) was isolated by ion exchange chromatography on DEAE-Sephacet. Cleavage of Cls heavy chain with CNBr yielded five fragments whose N-terminal sequences were determined. The alignment of the fragments within the heavy chain was established by tryptic peptides containing methionine. Cls heavy chain comprises about 470 amino acid residues and 42% of its sequence was determined. An intrachain sequence homology and a homology to the α² chain of human baptoglobin were identified. The C-terminal CNBr fragment comprising 44 amino acid residues was completely sequenced. From OMPS-skatole cleavage of reduced and alkylated Cls proenzyme a fragment was isolated which overlaps the Cls heavy and light chain parts and which contains the peptide bond cleaved during activation. The results show that this is an Arg-Ile bond and that under standard conditions of activation no peptide material is liberated from this portion of the molecule. The sequence data and homology to two-chain serine protcases indicate a single interchain disuluide bond in Cls. [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: |
Complementary Index |
