The total protein glycosylation profile and specific activity of lysosomal enzymes were investigated in rat submandibular glands isolated from very young (1-month), young (1.5-months) and adult rats (3-months) rats. The specific activity of lysosomal hydrolases (i.e. acid phosphatase, arylsulfatases A and B, β-N-acetyl-D-glucosaminidase, β-galactosidase and β-glucuronidase) decreased in parallel to increasing age of the animals. Furthermore, the thermal stability of acid phosphatase and β-N-acetyl-D-glucosaminidase was influenced by the age of rats. Age-related changes in protein profile regarding the intensity of particular bands as well as the appearance of certain proteins limited to special age groups were also demonstrated as revealed by Coomassie and lectin staining. Moreover, the marked age-related increase in structures Man (α1-2, α1-3, α1-6) Man, Fuc (α1-6) GlcNAc as well as Gal (β1-3) GlcNAc was observed, whereas staining with terminal NeuAc and GlcNAc showed an inverse correlation. The reaction with (β1-6) branched N-glycans and Gal (β1-3) Gal structures was limited to 1-month-old rats. No significant changes in a specific reaction with NeuAc (α2-3) Gal were observed. We speculate that the observed differences with respect to protein and glycosylation profiles between 1-month-old rats and older ones could be caused by a modification of the diet composition as well as by the functional and morphological maturation of the rat submandibular gland.