Extraction of streptococcal type 12 M protein by cyanogen bromide.

Abstract:

:Conditions for the release of streptococcal type 12 M protein from whole cells by cyanogen bromide are described; they demonstrated that methionine is not essential to the structural arrangements which account for some of its immunological and biological properties. The released M protein was separated from other proteins by column chromatography with hydroxylapatite. The type-specific molecules which reacted with precipitating antibodies were found only in the 0.3 M eluate, formed zones with mobilities less than 12% of that of the dye front on electrophoresis in the standard acrylamide disc gel system, formed at least four bands in sodium dodecyl sulfate-acrylamide disc gels with molecular weights ranging from 12,000 to 23,000, and stimulated the formation of opsonic antibodies in rabbits. Cyanogen bromide provides a highly specific method for the release of M proteins which should prove particularly useful in analyses of structural-functional relationships among different M proteins.

journal_name

Infect Immun

journal_title

Infection and immunity

authors

Vosti KL,Williams WK

doi

10.1128/IAI.21.2.546-555.1978

subject

Has Abstract

pub_date

1978-08-01 00:00:00

pages

546-55

issue

2

eissn

0019-9567

issn

1098-5522

journal_volume

21

pub_type

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