Crystallins

Some articles on crystallin, crystallins:

CRYAB
... (UCSC) Chr 11 111.78 – 111.79 Mb Chr 9 50.75 – 50.76 Mb PubMed search Alpha-crystallin B chain is a protein that in humans is encoded by the CRYAB gene ... Crystallins are separated into two classes taxon-specific, or enzyme, and ubiquitous ... Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins ...
Lens (anatomy) - Lens Structure and Function - Crystallins and Transparency
... Crystallins are water-soluble proteins that compose over 90% of the protein within the lens ... The three main crystallin types found in the human eye are α-, β-, and γ-crystallins ... Crystallins tend to form soluble, high-molecular weight aggregates that pack tightly in lens fibers, thus increasing the index of refraction of the lens while maintaining its transparency ...
Macromolecular Crowding - Importance
... A particularly striking example of the importance of crowding effects involves the crystallins that fill the interior of the lens ... be transparent precipitation or aggregation of crystallins causes cataracts ... Crystallins are present in the lens at extremely high concentrations, over 500 mg/ml, and at these levels crowding effects are very strong ...
CRYAA
... Alpha-crystallin A chain is a protein that in humans is encoded by the CRYAA gene ... Crystallins are separated into two classes taxon-specific, or enzyme, and ubiquitous ... cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins ...
CRYBB3
... (UCSC) Chr 22 25.6 – 25.6 Mb Chr 5 113.08 – 113.08 Mb PubMed search Beta-crystallin B3 is a protein that in humans is encoded by the CRYBB3 gene ... Crystallins are separated into two classes taxon-specific, or enzyme, and ubiquitous ... fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins ...