Antigens of the lens of Xenopus laevis

Campbell, John C.; Clayton, R. M.; Truman, D. E. S.

doi:10.1016/s0014-4835(68)80021-1

Cited by 37 publications

(7 citation statements)

References 20 publications

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“…We observed a gradual increase of the /3-crystallin components from stage 52, and like Campbell, Clayton and Truman (1968) we also found that in the adult X. Zuevis lens /3-crystallins form the bulk of the lens proteins. The two peaks we obtained in the &crystallin region by antigen-antibody crossed electrophoresis and immunoelectrophoresis show that this crystallin is heterogeneous and bears different antigenic properties.…”

Section: Discussionsupporting

confidence: 80%

“…The two peaks we obtained in the &crystallin region by antigen-antibody crossed electrophoresis and immunoelectrophoresis show that this crystallin is heterogeneous and bears different antigenic properties. Campbell et al (1968) have also reported that in Xenopus lens fi-crystallin fractions are complex molecules containing several antigens that exhibit partial immunological similarity with a line in the anodal end, and could be partially identical to some lines at the cathodal end in immunoelectrophoresis.…”

Section: Discussionmentioning

confidence: 91%

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Thin layer isoelectric focusing of the soluble lens extracts from larval stages and adult Xenopus laevis

Brahma

Bours

1972

Experimental Eye Research

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Soluble lens extracts from diEerent larval stages and a,lso from adult Xevus lue& were studied by thin layer isoelectric focusing.These lens extracts were also tested against antiserum to adult X. 1aeG.s total lens proteins by two-dimensional antigen-antibody crossed electrophoresis.By isoelectric focusing the lens crystallins were resolved into 13 major components. In the adult lens some components of the r-crystallins were lost, the /3-crystallins formed the major fraction and thea-crystallin appeared to be the weakest of the crystallin fractions.

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Section: Discussionsupporting

confidence: 80%

Section: Discussionmentioning

confidence: 91%

Thin layer isoelectric focusing of the soluble lens extracts from larval stages and adult Xenopus laevis

Brahma

Bours

1972

Experimental Eye Research

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“…For chick iris this cross-reactivity was already determined by LANGMAN & PRESCOTT (1959), ~ArSEI_ (1962, MA~SEL & HAR~rSON (1963a, b) and CLAYTON et al (1968). This strong cross-reactivity for iris was confirmed by the use of polyvalent antisera (BOURS, 1973a) and monospecific antisera (BOURS & VAN DOORENMAALEN, 1972) and was ascertained in this way for chick ~--, ~-, y-crystallins and FISC.…”

Section: Antigenic Properties Of Protehts Fi'om Chick #Re'a-ocular Tisupporting

confidence: 63%

“…Reviews on the comprehensive literature on this subject were published by CLAYTON et al (1968) and by BLOCH-MtCHEL (1970). The cross-reactivity of the antigens of the lens with the antigens of other ocular tissues can be shown in two ways: (1) immunological reaction of antiserum to lens crystallins with the antigens from intraocular tissues;…”

Section: Antigenic Properties Of Protehts Fi'om Chick #Re'a-ocular Timentioning

confidence: 99%

“…This result could be confirmed by column chromatography on Sepharose 6B at 4 ~ C, because we found the bovine pre-~-crystallin always in the ~t-crystallin fraction, which has an approximate molecular weight of around 80,000 (BOURS & BRAmdA, 1973). The pre-~.-crystallin is not merely present in bovine lens (SWANBORN, 1966), but also in amphibian lenses (ZVVAAN, 1963;CAMPBELL, CLAYTON & TRUMAN, 1968;BRAHMA & VAN DOORENMAALEN, 1969). We found that the pree-crystallin isolated from Rana esculenta lens extract is also localized in a ~-crystallin fraction of low molecular weight, at the same elution volume as the bovine pre-v.-crystallin (BOUleS & BRAHMA, 1973).…”

Section: Pre-~-crystallinmentioning

confidence: 99%

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Isoelectric focusing and immunochemistry of lens crystallins

Bours

1974

Doc Ophthalmol

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This is a review of 11 published articles with some conclusive results on the isoelectric focusing and immunochemistry of lens crystallins. The techniques used throughout the work are isoelectric focusing and immunological methods.The isoelectric focusing technique is performed on an analytical scale to realize the separation of proteins by isoelectric focusing in thin-layer polyacrylamide gels. The importance of carrying out all isofocusing techniques at 4 ~ C, and also of measuring the pH gradients established at the same temperature is noticed. Free isoelectric focusing is used as a preparative step to isolate uncontaminated crystallin fractions. Both analytical and preparative isoelectric focusing experiments of crystallins performed throughout the work are in absence of urea or any other dissociating medium.The purity of proteins isolated by free iseelectric focusing is examined by criteria of homogeneity which are founded on three different techniques, e.g. thin-layer isoelectric focusing, immunoelectrophoresis and antigen/antibody crossed electrophoresis.The existence of various crystallins in the chick lens, like ~z-, ~-crystallin and FISC, related to own data, is reviewed and nomenclatures of chick lens crystallins are compared with present data from literature. The antigenic properties of proteins from chick intra-ocular tissues are also discussed. Anti-total iris serum contains antibodies against crystallins and serum proteins. The presence of proteins immunologically identical to lens crystallins in chick iris is shown by indirect immunofluorescence experiments: brilliant fluorescence of the lens is observed due to the presence of crystallin antibodies in anti-total iris serum. It is concluded that proteins of all intra-ocular tissues which are immunologically identical to lens crystallins are essential structural elements. Contrary to this statement several authors support the theory that the presence of proteins immunologically identical to lens crystallins in the intra-ocular tissues is due to a post-mortem diffusion of these antigens from the lens. The presence of several erum proteins in all intra-ocular tissues excepting lens is shown. Evidence is presented that the number of serum proteins in intra-ocular tissues is restricted by the various blood/ocular barriers, and that the blood/retinal barrier is of the same nature as the blood/brain barrier.The presence ~-, ~-, ,,,-and pre-~-crystallins is shown in various stages of the bovine embryonic lens by thin-layer isoelectric focusing and various immunological methods. It is defined that the bovine -~,-crystallins have isoelectric points higher than pI --7.0. It is shown by immuno-osmophoresis that the embryonic ~-crystallins consist of two molecular forms with different electrophoretic mobilities. The ~-crystallins are forming half the total amount of the crystallins present in the embryonic lens. It is concluded that the "c-crystallins are more prominent in embryonic cow lens and in adult lens nucleus and less prominent in adult lens cortex. The...

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Studies on the water‐soluble lens proteins of the lizard, Calotes versicolor. II. Electrophoretic and immunological characterization

1982

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The Sephadex G-200 gel filtration fractions C1 to C6 of the water-soluble lens proteins of Calotes versicolor have been characterized by polyacrylamide gel electrophoresis (PAGE), 7 M urea PAGE, SDS PAGE, and immunological tests. C1 fraction, an alpha-crystallin which cross-reacts with chick alpha, has very low amount of B chains. It shows two bands in SDS PAGE, one strong and another weak. C2 and C3 fractions, both of which partially cross-react with chick beta-crystallins, are largely similar but not identical. C2 in SDS PAGE produces a faint band with a molecular weight of 54,500, which suggests that C2 may either contain a small amount of delta-crystallin in addition to beta H crystallin or that Calotes beta H has a high molecular weight subunit like human beta H; however, in immunological tests no material cross-reacting with chick delta was seen. C4 and C5 are low molecular weight, monomeric, and basic proteins which in all probability are not gamma-crystallins.

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Antigens of the lens of Xenopus laevis

Cited by 37 publications

References 20 publications

Thin layer isoelectric focusing of the soluble lens extracts from larval stages and adult Xenopus laevis

Thin layer isoelectric focusing of the soluble lens extracts from larval stages and adult Xenopus laevis

Isoelectric focusing and immunochemistry of lens crystallins

Studies on the water‐soluble lens proteins of the lizard, Calotes versicolor. II. Electrophoretic and immunological characterization

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