نتایج جستجو برای: crystallins

تعداد نتایج: 1695  

Journal: :Molecular Vision 2008
Mason Posner Molly Hawke Carrie LaCava Courtney J. Prince Nicholas R. Bellanco Rebecca W. Corbin

PURPOSE To characterize the crystallin content of the zebrafish lens using two-dimensional gel electrophoresis (2-DE). These data will facilitate future investigations of vertebrate lens development, function, and disease. METHODS Adult zebrafish lens proteins were separated by 2-DE, and the resulting spots were identified by matrix-assisted laser desorption/ionization time of flight mass spe...

Journal: :Investigative ophthalmology & visual science 1987
M S Swamy E C Abraham

Because of minimal or no turnover, lens proteins are subjected to substantial post-translational modifications which in turn disrupt lens architecture and change the optical properties leading to senile cataract formation. Progressive glycation is believed to have the potential to initiate the changes that are conducive to lens opacification. Fisher 344 rats were systematically followed from ju...

Journal: :The Biochemical journal 1995
S H Chiou C W Yu C W Lin F M Pan S F Lu H J Lee G G Chang

S-Crystallin is a major protein present in the lenses of cephalopods (octopus and squid). To facilitate the cloning of this crystallin gene, cDNA was constructed from the poly(A)+ mRNA of octopus lenses, and amplified by PCR for nucleotide sequencing. Sequencing of 10 of 15 positive clones coding for this crystallin revealed three distinct S-crystallin isoforms with 61-64% identity in nucleotid...

2017
Ales Cvekl Yilin Zhao Rebecca McGreal Qing Xie Xun Gu Deyou Zheng

The birth of novel genes, including their cell-specific transcriptional control, is a major source of evolutionary innovation. The lens-preferred proteins, crystallins (vertebrates: α- and β/γ-crystallins), provide a gateway to study eye evolution. Diversity of crystallins was thought to originate from convergent evolution through multiple, independent formation of Pax6/PaxB-binding sites withi...

Journal: :Investigative ophthalmology & visual science 2000
Y Nakamura C Fukiage M Shih H Ma L L David M Azuma T R Shearer

PURPOSE The purpose of the present experiments was to provide a biochemical mechanism for the involvement of lens-specific calpain Lp82 in experimental cataractogenesis in mice. METHODS Nuclear cataracts were produced by culturing lenses from 4-week-old mice and rats in calcium ionophore A23187 or by injection of buthionine sulfoximine (BSO) into 7-day-old mice. Casein zymography, sodium dode...

Journal: :Molecular biology and evolution 1985
Y Quax-Jeuken S Bruisten H Bloemendal W W de Jong E Nevo

The mole (Talpa europaea; Insectivora) and the mole rat (Spalax ehrenbergi; Rodentia) both have degenerated eyes as a convergent adaptation to subterranean life. The rudimentary eye lenses of these blind mammals no longer function in a visual process. The crystallin genes, which display a lens-specific expression pattern, were studied in these blind mammals and in related species with normal ey...

Journal: :Investigative ophthalmology & visual science 1978
M K Mostafapour V N Reddy

A method has been developed to isolate and characterize beta-crystallins of rabbit lens cortex. Chromatographic separation of water-soluble structure proteins of rabbit lens cortex on a Sephacryl S-200 gel column yielded four beta-crystallin peaks (beta1, beta2, beta3 and beta4), all eluting between alpha and gamma-crystallins. Their molecular weights were estimated to be 250,000, 130,000, 60,0...

Journal: :Integrative and comparative biology 2003
Joram Piatigorsky

The crystallins comprise 80-90% of the water-soluble proteins of the transparent, cellular, refractive eye lens and are responsible for its optical properties. Comparative studies have established that the crystallins are surprisingly diverse and often differ among species in a taxon-specific fashion. In general, the crystallins are derived from or identical to metabolic enzymes or stress (smal...

Journal: :The Journal of biological chemistry 1994
L R Miesbauer X Zhou Z Yang Y Sun D L Smith J B Smith

Post-translational modifications of the water-soluble human lens crystallins from young adult donors were identified and located using electrospray ionization mass spectrometric analysis of the intact proteins and fast atom bombardment mass spectrometry of enzymatic digests. Peptides corresponding to all of the sequences of alpha A-, alpha B-, and beta B2-crystallins were found, permitting the ...

Journal: :Experimental Eye Research 1989

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