小牛晶状体晶状体蛋白中非色氨酸发色团的分子定位。

The molecular localization of non-tryptophan chromophores in calf lens crystallins.

作者信息

Pulcini D, Stiuso P, Miele L, Della Pietra G, Colonna G

机构信息

Department of Biochemistry and Biophysics, University of Naples, Italy.

出版信息

Biochim Biophys Acta. 1989 Mar 16;995(1):64-9. doi: 10.1016/0167-4838(89)90234-3.

DOI:10.1016/0167-4838(89)90234-3

PMID:2923916

Abstract

A single-step separation of calf lens gamma-crystallin into six protein components is described. UV absorption spectra, characterized by the presence of high absorbance in the 240-250 nm and 310-360 nm spectral regions as well as by fluorescence emission above 400 nm, are shown by six components. alpha-, beta and beta S crystallins have been compared with the gamma-fraction for the presence of non-tryptophan fluorescence. The chromophores responsible for this non-tryptophan fluorescence were found to be associated with gamma-crystallin components only. The spectral features of one selected gamma-crystallin component (characterized by an isoelectric point of 7.68) have been examined. Results seem to suggest the presence of oxidative products of tryptophan. Implications of these findings for the expression of human and bovine genes are also considered.

摘要

本文描述了一种将小牛晶状体γ-晶状体蛋白一步分离为六种蛋白质成分的方法。六种成分均显示出紫外吸收光谱，其特征在于在240 - 250nm和310 - 360nm光谱区域存在高吸光度，以及在400nm以上有荧光发射。已将α-、β-和βS-晶状体蛋白与γ-组分进行比较，以检测非色氨酸荧光的存在。发现负责这种非色氨酸荧光的发色团仅与γ-晶状体蛋白成分相关。已研究了一种选定的γ-晶状体蛋白成分（其特征在于等电点为7.68）的光谱特征。结果似乎表明存在色氨酸的氧化产物。还考虑了这些发现对人类和牛基因表达的影响。