Biochemical study on some acid hydrolases in the normal rabbit cornea.
The activities of acid phosphatase, beta-glucuronidase, beta-galactosidase, and N-acetyl-beta-D-glucosaminidase were investigated in the normal rabbit cornea. For all spectrophotometric assays, appropriate p-nitrophenyl derivates were used. Only beta-glucuronidase were determined employing phenolphthalein glucuronid as a substrante. Acid phosphatase revealed the highest activity, followed by N-acetyl-beta-D-glucosaminidase and beta-galactosidase. In the case of beta-glucuronidase the lowest activity was found. The results on the rabbit cornea are compared with those on some other tissues described in the literature. Correlation of biochemical data and histochemical findings in the same species is briefly discussed.
D000118:Acetylglucosaminidase / Q000378:metabolism; D000135:Acid Phosphatase / Q000378:metabolism; D000818:Animals; D003315:Cornea / Q000201:enzymology*; D005696:Galactosidases / Q000378:metabolism; D005966:Glucuronidase / Q000378:metabolism; D006867:Hydrolases / Q000378:metabolism*; D008247:Lysosomes / Q000201:enzymology; D011817:Rabbits
D006867:Hydrolases; D000135:Acid Phosphatase; D005696:Galactosidases; D005966:Glucuronidase; D000118:Acetylglucosaminidase