Huang Q L, Russell P, Stone S H, Zigler J S
Curr Eye Res. 1987 May;6(5):725-32. doi: 10.3109/02713688709034836.
Lens proteins from the guinea pig (Cavia porcellus) were found to be similar to those of other mammals with the exception of the presence of a previously undescribed constituent comprising about 10% of the total soluble lens proteins. This oligomeric protein is composed of polypeptides with apparent molecular weight of 38,000 and elutes from gel exclusion chromatography columns in the beta H-crystallin fraction. Following purification by ion exchange chromatography an antibody was raised against the protein. Using that antibody and antibodies specific for other crystallins we could detect no cross-reactivity between the guinea pig protein and any other reported lens crystallin. This protein, which we have named zeta (zeta)-crystallin, is the first reported mammalian lens crystallin which is not part of the alpha- or beta-gamma families of crystallins. Unlike all other known mammalian crystallins, which have little or no alpha-helical structure, zeta-crystallin is estimated to be approximately 30-40% alpha-helix.
豚鼠（Cavia porcellus）晶状体蛋白被发现与其他哺乳动物的晶状体蛋白相似，但存在一种先前未描述的成分，该成分约占晶状体总可溶性蛋白的10%。这种寡聚蛋白由表观分子量为38,000的多肽组成，并从凝胶排阻色谱柱中在βH-晶状体蛋白部分洗脱。通过离子交换色谱纯化后，制备了针对该蛋白的抗体。使用该抗体和针对其他晶状体蛋白的特异性抗体，我们未检测到豚鼠蛋白与任何其他已报道的晶状体蛋白之间存在交叉反应。这种我们命名为ζ（zeta）-晶状体蛋白的蛋白质，是首个被报道的不属于α-或β-γ晶状体蛋白家族的哺乳动物晶状体蛋白。与所有其他已知的几乎没有或没有α-螺旋结构的哺乳动物晶状体蛋白不同，ζ-晶状体蛋白估计约30-40%为α-螺旋结构。
