Study of the lens capsule synthesis

Study of the lens capsule synthesis

1W A l~sl’lLxc”I’s a number of proteins immunologically identical to lens crystallins like x-cryst~allin, S-crystallin and /&crystallins (BOWS, 1974...

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1W

A l~sl’lLxc”I’s

a number of proteins immunologically identical to lens crystallins like x-cryst~allin, S-crystallin and /&crystallins (BOWS, 1974). By immunoelectrophoresis of cornea1 extract against chick serum ant,iserum, a number of serum proteins are detected like albumin, immunoglobulin (:. and follr unidentified proteins which are not immunoglobulins (Bours, 1973s). Localization of serum proteins in chick cornea is made by t,he indirect imn~urlofi~~orc~s~er~(~c staining technique. When chick serum antiserum is applied, serum proteins are localized in thr cornea1 stroma, the Bowman’s layer and in the endothelium. Using a monovalent’ antiserum to serum albumin, albumin is localized in the cornea1 endothelium which is strongly positive. while the stroma and the epithelium are negative (Bours, 1973b). Soluble extracts of the cornea1 endothelium and epithelium are made after dissecbion of these tissues from the chick adult cornea. As detected by immunoelectrophoresis with polyvalent antisera, the endothelial extract contains albumin, immunoglobulin G, two unidentified proteins which are not immunoglobulins, and proteins immunologically identical to lens p-cryst,allins. The epithelial extract contained only a protein immunologically identical t)o chick lens “y”crystallin, and no serum proteins. In immunofluorescence experiments of early embryonic stages from 4 days up to 14 days, the Bowman’s layer shows a strong positive reaction using antiserum to total cornea extract. while in the hatched state this reaction is absent. Similar observations were made by using an ant’iserum specific to serum albumin (Bours, 1973b).

Bours, Bours, Bours, Bours,

J. J. J. J.

(1971). (1973a). (1973b). (1974).

REFERENCES J. Chromutog. 60, 225. Exp. Eye Res. 15,299. Exp. Eye Res. 16,487. Dccum. Ophthnlmol. 37, 1.

Study of the Lens Capsule Synthesis (exhibit) P. KERK,

Paris