Summary
Proteins are substances on which the organic composition and structure of the cell depends. The protein concentration of the crystallin lens is higher than that of any other organ of the body. This predominance of proteins in the lens' substance points clearly towards the cardinal role they play in the metabolism of this organ. The present review is concerned with the problem of protein chemistry of the lens and mainly with the determination of the amino acid composition of the lenticular proteins. Such determinations were made on the undivided total proteins or on the isolated individual proteins.
The lens' substance consists partly of an insoluble albuminoid and partly of two water-soluble proteins called α- and β- crystallins. Besides, there is a small amount of albumin. The quantitative presence of nucleprotein was also demonstrated. This latter substance seems to occur in the lens mainly in the form of ribonucleic acid, suggesting a significant protein metabolism. The soluble fractions of the lens' proteins are diminishing with advancing age while the insoluble fraction is increasing: a phenomenon which might explain the loss of plasticity of the lens in higher age.
The amino acid composition of both the total undivided proteins and the divided individual proteins of the crystallin lens was estimated by a few investigators. The data obtained are tabulated and compared. A close harmony of the results of recent investigators evidences the reliability of the results obtained. Thus, the protein chemistry of the lens, though still in its early stage, can already be considered as a valuable approach to biochemical problems of this organ. There can hardly be any doubt that the crystallin lens has a considerable protein metabolism. Diets deficient in protein or in an essential amino acid lead to cataract formation. The method of delayed supplementation of an essential amino acid demonstrated that cataract formation is exclusively the result of disturbed protein synthesis, evidencing this primary “protein function” of amino acids. An “extra protein function”, such as formation of vitamins, co-enzymes, hormones or other unknown substances, was not as yet demonstrated in the lens. The experimental production of nutritional (protein and amino acid deficiency) cataracts suggests the possibility that in the formation of human senile cataracts, nutritional irrationalities play an important role. Faulty consideration of the age, just as in infants, may lead to forms of malnutrition, which in the long run contribute to the development of cataract.
The proteins of the cornea and sclera have been similarly analyzed, their amino acid composition determined, and the results comparatively tabulated.
Résumé
La concentration en protides est plus élevée dans le cristallin que dans n'importe quel autre organe. Ce fait permet de supposer que les protides jouent un rôle de premier plan dans le métabolisme de la lentille.
Dans cette revue d'ensemble il est question de la chimie des protides du cristallin et surtout de la détermination de leurs acides aminés. Ceux-ci ont été analysés en partant du cristallin entier ou des diverses fractions protidiques. Les résultats obtenus par les différents auteurs sont réunis et comparés. On peut conclure à une bonne concordance des chiffres publiés par les chercheurs modernes.
Il n'est pas douteux que la lentille possède un métabolisme protidique considérable. Des régimes carencés en protides ou en un acide aminé essentiel donnent lieu à la formation de cataractes. Celles-ci sont sûrement la conséquence d'un trouble de la synthèse protidique. Il n'est pas impossible que certains régimes, mal appropriés à l'âge du malade et prolongés pendant des années, jouent un rôle dans le développement de la cataracte sénile humaine.
Finalement, les protides de la cornée et de la sclérotique sont également passés en revue et les résultats des examens chimiques portant sur les acides aminés sont juxtaposés.
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Schaeffer, A.J. Some problems of protein chemistry of the eye. Doc Ophthalmol 5, 403–451 (1951). https://doi.org/10.1007/BF00143666
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DOI: https://doi.org/10.1007/BF00143666