Bessems G J, De Man B M, Bours J, Hoenders H J
Exp Eye Res. 1986 Dec;43(6):1019-30. doi: 10.1016/0014-4835(86)90079-5.
The native water-soluble proteins of equator, anterior cortex, posterior cortex and nucleus from bovine lenses in the age range 0.3-33.7 years were analyzed by high-pressure gel-permeation chromatography and high-pressure ion-exchange chromatography. Unlike the equator and cortices, the nucleus shows a gradual decrease in alpha-crystallin proportion with age which is not compensated for by an increase in HM-crystallin. The beta 6H-crystallin species, almost the only beta H-component in the youngest lens, is largely replaced by at least four fractions with higher and lower molecular weights in the older lenses. In the nucleus a beta L-component (39,000 MW) increasingly seems to replace the major beta L-crystallin (beta 2L, 50,000 MW). Moreover, a switch in the synthesis of monomeric crystallins is demonstrated. This study clearly reveals an age-related increase in the size heterogeneity of the native soluble crystallins with age.
采用高压凝胶渗透色谱法和高压离子交换色谱法，对年龄在0.3至33.7岁之间的牛晶状体赤道部、前皮质、后皮质和核中的天然水溶性蛋白质进行了分析。与赤道部和皮质不同，核中α-晶状体蛋白的比例随年龄逐渐下降，且未被HM-晶状体蛋白的增加所补偿。β6H-晶状体蛋白几乎是最年轻晶状体中唯一的βH成分，在较老的晶状体中，它在很大程度上被至少四种分子量较高和较低的组分所取代。在核中，一种βL成分（39,000 MW）似乎越来越多地取代了主要的βL-晶状体蛋白（β2L，50,000 MW）。此外，还证实了单体晶状体蛋白合成的转变。这项研究清楚地揭示了天然可溶性晶状体蛋白的大小异质性随年龄增长而增加。
