Abstract
Chemical studies on the organ specificity were performed using
TABLE XIV Effect of Esterification of Carboxyl Groups in the Partial Hydrolysate of Eyelens Crystallin upon Its Activity as An Inhibitor
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eyelens crystallin of ox, horse, and pig and the following results were obtained:
1. Sphingomyelin, cerebroside, and other lipids contained in .the eyelens are not responsible for the organ specificity.
2. α- and β-Crystallins of eyelens react specifically, but γ-crystallin does not.
3. The ability of the crystalline to react with the eyelens antiserum is lost by hydrolysis with 1 N or 5 N sulfuric acid for 0.5 or 0.3 hours, but the activity of inhibiting the serological reaction between lens crystallin and the corresponding antibodies remains intact when it was hydrolysed with 5 N sulfuric acid for one hour.
4. These partial hydrolysates scarecely show biret reaction but are not precipitated by sulfosalicylic or trichloroacetic acid, and can be dialyzed throughly collodium membran.
5. When the partial hydrolysate is coupled with diazobenzene-sulfanylic acid or the free carboxyl groups in it are esterified with ethyl groups the activities are destroyed.
6. The active substances in the partial hydrolysates of the eyelens crystallins of ox or horse can be isolated by column chromatography, and by the complete hydrolysation, they liberate several amino acids common to all, other such as serine, histidine, glutamic acid, alanine, and tyrosine.
From these facts, it may be considered that the specific substances in eyelens of animals are α- and β-crystallins and the chemical structures which is responsible for organ specificity are groups of comparatively small polypeptide residues.
The author wishes to express his most sincere thanks to prof. S. Fujimura for his kind advises through this research.
