CHANGES IN THE LOW MOLECULAR WEIGHT NITROGENOUS COMPOUNDS OF EXCISED BOVINE MUSCLE

Investigations were completed to determine whether any differences could be detected in the low molecular weight nitrogenous compounds of excised bovine muscle at O-time or that held at 4° C for 12 days. No differences were noted between the electrophoretic patterns of the soluble proteins of the 0 and 12day samples either before or after gel filtration on Sephadex G-25 columns. However, gel electrophoretic patterns indicated that one band consisted of low molecular weight non-protein compounds. Absorbance data (280 and 260 nm) of the soluble proteins separated by gel filtration indicated that the 12day sample contained a slightly higher level of low molecular weight nonprotein nitrogenous compounds than did the O-day sample. Results of nitrogen determinations of the gel-filtered extracts also supported this finding. Data of ultraviolet scanning of gel-ftltered extracts showed that the low molecular weight nitrogenous compounds had a greater absorbancy at 260 than at 280 nm. Results of two-dimensional paper chromatography-high voltage electrophoresis did not reveal the presence of polypeptides in either the O- or 12day samples.