The insoluble proteins of bovine crystalline lens

Absorption experiments as well as organ-specific cross-reactions were used for immunochemical comparison of human normal and senile cataract lens. All the experiments revealed an identity of antigenic specificities in the crystallin as well as in the albuminoid fractions of human normal and senile cataract lenses. The human senile cataract lens crystallins contained a decreased amount of at least one immunologically specific β-crystallin antigen. A similar observation was made previously in experimental galactose cataract which occurs only in the young. The potential role of this protein in albuminoid formation is discussed. Under equal immunization procedures the cataract lens proteins tended to produce a stronger antibody response than the normal ones.

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“…Albuminoid solutions were prepared according to R uttf.nbf.ro [15] Immune sera. Immune sera were prepared in adult chinchilla rabbits (5-6 lb.)…”

Section: Methodsmentioning

confidence: 99%

Immunochemical Studies on Crystallins and Albuminoids in Human Senile Cataracts

York¹,

Martínez²,

Manski³

1972

Ophthalmic Res

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“…Studies by other investigators (22,23) also supported the conclusion that the insoluble protein fraction is mainly a polymerization product of some soluble fractions in which the transformation does not involve the -SH groups. However, work conducted by Testa, showed that incubation of lens proteins in oxygen does lead to the formation of -SS-groups.…”

Section: Resultsmentioning

confidence: 71%

Technical Progress Report, July 1, 1971--August 1, 1972.

1972

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This report summarizes results of studies on the chemical and conformational changes produced in proteins after gamma irradiation. Three different protein systems have been used: dry solid egg white lysozyme, a lysozyme DNA complex, and rabbit eye lens. The latter two systems have been studied on a preliminary level. Salt fractionation procedures followed by slab gel electrophoresis has been used to separate damaged and undamaged molecules. Results on irradiated solid lysozyme demonstrate that main chain fission occurs on irradiation, as well as crosslinking and chemical changes leading to destruction of conformation.

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“…Previous investigators [1,2,4,5] have described the presence of a-crystallin in insoluble protein; how ever, except for M a n sk i, Behrens and M a r tin ez [6] they could not detect /?-crystallin. These investigators concluded that bovine insoluble protein con tained pre-a-crystallin in addition to a-crystallin and ^-crystallin.…”

Section: Discussionmentioning

confidence: 96%

“…These studies [1][2][3][4][5][6], using immunolo gical and chromatographic techniques, have indicated that there is a structural resemblance between a-crystallin and insoluble protein from the bovine lens. Studies on the insoluble protein obtained from rat and dogfish lens have shown that it is very similar to the soluble/-crystallin fraction [7,8], So far, all the studies on the insoluble protein from different species have been carried out by solubilizing the insoluble protein either by 7 M urea or 1M alkali.…”

Section: Introductionmentioning

confidence: 99%

Immunochemical Relationship between Soluble and Insoluble Lens Proteins

Mehta¹,

Lerman²

1970

Ophthalmic Res

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The relationship between soluble and insoluble proteins in the bovine, human and dogfish lens has been studied by immuno-electrophoresis and urea starch gel electrophoresis at pH 3.0. The result from the immuno-electrophoresis experiment indicated that insoluble protein derived from bovine and human lens is composed of α- and β-crystallins while that obtained from dogfish lens contains γ- and β-crystallins. The urea starch gel electrophoretic patterns of α-crystallin and insouble protein in bovine and human lens showed considerable similarity, however, those of dogfish γ-crystallin and dogfish insoluble protein showed significant differences in their mobilities. The cross-reaction between bovine α-crystallin and bovine insoluble suspension was studied by the quantitative complement fixation test, using rabbit antisera to bovine α-crystallin. The results indicated that 5 to 10% of the total insoluble protein has α-crystallin in a form available for the reaction with the antibody. Similar results were observed when dogfish γ-crystalin and dogfish insoluble suspension was studied.

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The insoluble proteins of bovine crystalline lens

Cited by 37 publications

References 17 publications

Immunochemical Studies on Crystallins and Albuminoids in Human Senile Cataracts

Immunochemical Studies on Crystallins and Albuminoids in Human Senile Cataracts

Technical Progress Report, July 1, 1971--August 1, 1972.

Immunochemical Relationship between Soluble and Insoluble Lens Proteins

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