The aim of the current study was to demonstrate glycation of β<sub>L</sub>-, β<sub>S</sub>- and γ-crystallins in the young bovine lens. To establish which of the crystallins are glycated and where they are located in the lens, we carried out microsectioning of the lens, followed by isoelectric focusing (IEF). Four bovine lenses of 1.183 ± 0.070 years were frozen-sectioned into equator and 11 layers. Water-soluble crystallins were separated by IEF and stained: (1) with Coomassie brilliant blue for proteins; (2) with the lectin concanavalin A, followed by horseradish peroxidase and diaminobenzidine, for glycated proteins. Experiments were performed with crystallins and proteins in native form, in the absence of denaturants. The crystallins were separated by IEF into α-crystallins of high molecular weight (HM), α<sub>L</sub>-, β<sub>H</sub>-, β<sub>L</sub>-, β<sub>S</sub>- and γ-crystallins. In the lectin staining experiments, only HM, β<sub>L</sub>-, β<sub>S</sub>- and γ-crystallins were positive, whereas the α<sub>L</sub>- and β<sub>H</sub>-crystallins were negative. Contrary to the glycated γ-crystallins in the lens nucleus, the β<sub>S</sub>- and β<sub>L</sub>-crystallins were predominantly glycated in the anterior cortex and to a somewhat lower extent also in the posterior cortical regions. The degree of glycation (total densitometric readings of lectin-stained bands/Coomassie-blue-stained bands) is as follows: total γ-crystallins 2.44, β<sub>S</sub>-crystallins 0.77 and β<sub>L</sub>-crystallins 0.28. Though glycation in the bovine lens is very low, lectin staining is sufficiently sensitive to detect the various glycated crystallins. The degree of glycation of γ-crystallins was 3 times higher than that of β<sub>S</sub>-crystallins and 9 times higher than that of β<sub>L</sub>-crystallins.