Takemoto L
Division of Biology, Kansas State University, Manhattan 66506, USA.
Exp Eye Res. 1995 Dec;61(6):743-8. doi: 10.1016/s0014-4835(05)80025-9.
A previous study has demonstrated that in vivo, the peptide bonds at the C-terminal region of the alpha-A crystallins were cleaved in an age-dependent manner, between the two hydroxyl-containing amino acids in the sequence -PS(T)S (Takemoto, 1995). Bovine beta B2 crystallin also contains the sequence-PSS at its C-terminus. To determine if this specific site of cleavage occurred in other lens proteins besides alpha-A crystallin, beta B2 crystallin was prepared from total proteins of young versus adult bovine lens fiber cells. After cleavage by cyanogen bromide, the C-terminal fragments were characterized by mass spectrometry. The results showed that peptide cleavage also occurred between the two hydroxyl-containing amino acids in the sequence -PSS of beta B2 crystallin from older fiber cells, demonstrating that age-dependent cleavage of this peptide bond occurs in multiple proteins of the aging lens.
先前的一项研究表明,在体内,α-A晶状体蛋白C端区域的肽键在-PS(T)S序列中两个含羟基的氨基酸之间以年龄依赖性方式被切割(武本,1995年)。牛βB2晶状体蛋白在其C端也含有-PSS序列。为了确定除α-A晶状体蛋白外,这种特定的切割位点是否也发生在其他晶状体蛋白中,从幼年和成年牛晶状体纤维细胞的总蛋白中制备了βB2晶状体蛋白。用溴化氰切割后,通过质谱对C端片段进行了表征。结果表明,来自老年纤维细胞的βB2晶状体蛋白序列-PSS中两个含羟基的氨基酸之间也发生了肽段切割,这表明这种肽键的年龄依赖性切割发生在老化晶状体的多种蛋白质中。