IDENTIFICATION OF THE IN-VIVO TRUNCATION SITES AT THE C-TERMINAL REGION OF ALPHA-A CRYSTALLIN FROM AGED BOVINE AND HUMAN LENS
IDENTIFICATION OF THE IN-VIVO TRUNCATION SITES AT THE C-TERMINAL REGION OF ALPHA-A CRYSTALLIN FROM AGED BOVINE AND HUMAN LENS
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DOI：
10.3109/02713689508995806
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发表时间：
1995-09-01
影响因子：
2
通讯作者：
TAKEMOTO, LJ
中科院分区：
文献类型：
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作者：
TAKEMOTO, LJ
总α-A晶体蛋白从年轻的Versus老的透镜中纯化，然后用溴化氰消化。激光解吸质谱的C-末端片段表明，从牛和人的透镜的α-A晶体蛋白的C-末端的一个和五个氨基酸的年龄依赖性损失。这些结果表明，在正常透镜的老化过程中，α-A晶状体蛋白的特异性肽键被裂解。C-末端区域在序列-P-S（T）-S-中存在的两个含羟基氨基酸之间的两个位置被切割。
Total alpha-A crystallin was purified from young Versus old lens, followed by digestion with cyanogen bromide. Laser desorption mass spectrometry of the C-terminal fragment demonstrated age-dependent loss of one and five amino acids from the C-terminus of alpha-A crystallin from both bovine and human lens. These results demonstrate specific peptide bonds of alpha-A crystallin are cleaved during the aging process of the normal lens. The C-terminal region is cleaved in two places between the two hydroxyl-containing amino acids present in the sequence -P-S(T)-S-.