[IR-spectra of skeletal muscle mitochondria and endoplasmic reticulum]

The existance of alpha- and beta-protein conformation in human straight abdomen muscle mitochondria and microsomal fraction was established. The stability of beta-conformation was provided by hydrophobic and lipid protein interactions. The band at 1730 cm-1, C=O stretching of the carboxyl groups, was more intensive in mitochondria, presented in microsomal fraction and disappeared after its isooctane treatment. From the reducing of NH, OH stretching frequency in microsomes films, was made a conclusion that hydrogen bonds were stronger in that membrane.