Raman and infrared studies of homogeneous forms of acid phosphatase from rat liver.
Raman spectra of acid phosphatase (orthophosphoric-monoester phosphohydrolase (acid optimum), EC 3.1.3.2) forms from rat liver in water solution, and infrared spectra of the same forms as thin films, have been investigated. The spectra show strong bands belonging to phosphodiester or phosphomonoester residues. These groups are modified during the postsynthetic modification of acid phosphatase and are probably connected with the process of bonding and splitting of mannose 6-phosphate and N-acetylglucosamine, in agreement with previous biochemical models for the intracellular transport of newly synthesized lysosomal hydrolases to lysosomes. Some other bands in the infrared spectra are assigned to vibrations of N-H groups which may belong to N-acetylglucosamine.
D000135:Acid Phosphatase / Q000032:analysis*; D000818:Animals; D007527:Isoenzymes / Q000032:analysis*; D008099:Liver / Q000201:enzymology*; D051381:Rats; D011919:Rats, Inbred Strains; D013055:Spectrophotometry, Infrared; D013059:Spectrum Analysis, Raman
D007527:Isoenzymes; D000135:Acid Phosphatase