Isolation and characterization of four basic proteins from horse eosinophilic granules.

Abstract:

:Four new basic proteins were isolated from horse eosinophils and purified. The eosinophils release these proteins after permeabilization with saponin and degranulation stimulized by guanosine 5'-O-thiotriphosphate. The proteins were separated and purified on a Superose P12- and a Mono S-column by fast protein liquid chromatography. The amino acid composition, the relative molecular mass, the isoelectric point and the partial N-terminal sequence of the four proteins were determined. Papain-activation and ribonuclease activity of the four proteins were tested for comparison with the human eosinophil basic granular proteins. The cytotoxicity of the hole granular extract and of the isolated basic proteins against Escherichia coli K12 was also studied.

authors

Piller K,Portmann P

doi

10.1006/bbrc.1993.1425

subject

Has Abstract

pub_date

1993-04-30 00:00:00

pages

373-80

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(83)71425-7

journal_volume

192

pub_type

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