Far infrared spectra of acid phosphatase from rat liver. Spectra of the native and the heat- and acid-denatured isoenzymes.
The spectrum of acid phosphatase, as well as that of its isoenzymes, shows in the region 100-500 cm-1 a band at 362 cm-1 which appears to be due to second-order structure (alpha-helix). The character of these spectra is unchanged by deuteration of the protein. Heat- and acid-denaturation affected all the spectra studied pointing to the occurrence of conformational changes, but a close similarity between the spectra of the two isoenzymes was consistently observed.
D000135:Acid Phosphatase / Q000032:analysis*; D000818:Animals; D006358:Hot Temperature; D006851:Hydrochloric Acid / Q000494:pharmacology; D007527:Isoenzymes / Q000032:analysis*; D008099:Liver / Q000201:enzymology*; D008968:Molecular Conformation; D008970:Molecular Weight; D051381:Rats; D013055:Spectrophotometry, Infrared
D007527:Isoenzymes; D000135:Acid Phosphatase; D006851:Hydrochloric Acid