闈舵爣锛欬p style="text-indent: 2em;">CRYGB

浜у搧鍒悕锛欬p style="text-indent: 2em;">CRYG2锛 CTRCT39锛 CRYGB锛 crystallin gamma B锛 crystallin gamma B锛 gamma-crystallin B锛 crystallin, gamma 1-2锛 鏅剁姸浣撹泲鐧轿矪纬B-crystallin锛

鑳屾櫙淇℃伅锛欬div style="text-indent: 2em;">Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. Four gamma-crystallin genes (gamma-A through gamma-D) and three pseudogenes (gamma-E, gamma-F, gamma-G) are tandemly organized in a genomic segment as a gene cluster. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation.