13q-/r(13) mosaicism

Tamura, Takashi; Umetsu, Masao; Motoya, Hisashi; Niikawa, Norio

doi:10.1007/bf00441721

Cited by 1 publication

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“…Euglobulin precipitates can be prepared by dialysis or dilution of serum with low-ionic-strength buffers of varying pH. The method of Tamura & Nelson (1968), with sodium phosphate buffer, pH7.5, I 0.04, was attempted, but this was found to result in substantial activation ofsubcomponent C1 s to Cls. In the method of isolation of human subcomponent Cls reported by Valet & Cooper (1974), a critical factor of the purification schedule is the formation of the euglobulin by dialysis at acid pH and at 0°C.…”

Section: Resultsmentioning

confidence: 99%

The purification and characterization of subcomponent C1s of the first component of bovine complement

Campbell¹,

Booth²,

Fothergill³

1979

Biochemical Journal

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Bovine C1s, a subcomponent of the first component of complement, was purified in good yield by a combination of euglobulin precipitation and ion-exchange and molecular-sieve chromatography. Approx. 10 mg can be obtained from 3 litres of serum, representing a yield of 11%. The C1s is obtained in zymogen form, with a mol.wt. of 85000-88000, determined by gel filtration and SDS/polyacrylamide-gel electrophoresis. It is haemolytically active when tested with human C1q and C1r. Activation can be achieved by incubation with human C1r, resulting in cleavage of the C1s chain into two chains of 65000 and 27000 mol.wt. and the generation of an isoleucine N-terminal residue on the smaller chain. Active C1s binds an equimolar amount of di-isopropyl phosphorfluoridate to the smaller chain, which is the C-terminal part in the zymogen. The chains can be separated by ion-exchange in 8 M-urea. All of these characteristics show that bovine C1s is very similar to its human counterpart.

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Section: Resultsmentioning

confidence: 99%