Detail of "80295-56-3"

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C6 [complement] phenotyping in sera and bloodstains by isoelectric focusing followed by electroimmunoblotting

C6 [complement] phenotyping in sera and bloodstains by isoelectric focusing followed by electroimmunoblotting. Oya, M.; Kido, A.; Ose, Y.; Komatsu, N. (Dep. Legal Med., Yamanashi Med. Univ., Tamaho 409-38, Japan). Forensic Sci. Int., 33(1), 61-7 (English) 1986. CODEN: FSINDR. ISSN: 0379-0738. DOCUMENT TYPE: Journal CA Section: 4 (Toxicology) The genetic polymorphism of C6 [80295-56-3] complement was investigated in 329 unrelated Japanese individuals by using isoelec. focusing in polyacrylamide gels followed by an electroimmunoblotting technique. Besides 6 common phenotypes C6 A, AB, B, AB2, BB2, and B2 6 rare variants were obsd. The allele frequencies were: C6*A = 0.4422, C6*B = 0.4757, C6*B2 = 0.0714, C6*A3 = 0.0015, C6*M1 = 0.0046, and C6*B3 = 0.0046. The population data confirmed that the C6*B2 allele is the 3rd common allele characterizing Japanese. The present electroimmunoblotting technique was applied to demonstrate C6 types in dried blood stains. The C6 types were detd. from bloodstains stored at 4° for ￡10 wk, at room temp. for ￡2 wk, and at 37° for ￡4 days. This component system offers a new powerful means for the medicolegal grouping of bloodstains.

Activation of the fifth component of human complement, C5, without cleavage, by methionine oxidizing agents

Activation of the fifth component of human complement, C5, without cleavage, by methionine oxidizing agents. Vogt, W.; Zimmermann, B.; Hesse, D.; Nolte, R.In this study， 63-68-3 and 80295-56-3 are also used. (Max Planck Inst. Exp. Med., Goettingen D-3400, Germany). Mol. Immunol., 29(2), 251-6 (English) 1992. CODEN: MOIMD5. ISSN: 0161-5890. DOCUMENT TYPE: Journal CA Section: 15 (Immunochemistry) Purified human complement C5 was incubated with chloramine T (Cl-T) or N-chlorosuccinimide (N-Cl-S) in barbital buffer, pH 7.2. The treatment led to C5 activation: Cl-T- and N-Cl-S-treated C5 acquired a binding site for C6; upon incubation with C6 and subsequent addn. of C7, C8, and C9 a membrane attack complex formed which lysed nonsensitized guinea pig red cells (reactive lysis). While the physiol. activation of C5 follows its specific cleavage, the resulting fragment C5b representing the activated C5 and expressing the C6 binding site, the treatment with the mentioned chems. does not lead to fragmentation of the C5 protein. So, functionally, the product of the chem. treatment is C5b-like, but chem., it comprises the whole protein; no C5a is released. Cl-T and N-Cl-S are known to more or less selectively oxidize methionine residues in proteins, dependent on the conditions. Other sensitive amino acid residues are tryptophan and cysteine. Conditions were chosen for treatment of C5 with Cl-T which exclude attack on tryptophan, and it was ensured that human C5 does not contain free cysteine residues. Further, oxidn. of about 60% of the methionine residues of C5 by Cl-T was demonstrated by amino acid anal. All evidence thus points to methionine residue(s) as the site of attack of Cl-T and probably also of N-Cl-S. The oxidn. product of methionine, its sulfoxide, may cause a change in structural conformation of C5 which involves expression of the C6 binding site. Earlier it was found that oxidn. of C5 by hydroxyl radicals leads to its activation without cleavage. Since the properties of this C5b-like product resemble those of the product of treatment with Cl-T and N-Cl-S, it is suggested that the formerly found activation of human C5 by hydroxyl radicals is also mediated by oxidn. of methionine residue(s) in the C5 protein. .