Graduate Thesis Or Dissertation
 

Proteolytic and chemical changes of some minor nitrogen compounds and extra protein of bovine muscle during aging

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  • Investigations were conducted to determine whether the low molecular weight nitrogen compounds and the extra protein complex of bovine psoas major muscle were altered during a 12-day aging period. Electrophoretic studies of soluble proteins either before or after gel filtration on Sephadex G-25 columns indicated that the soluble proteins were not altered during 12 days of aging. Data of absorbance measurements (280 and 260 nm) of the soluble protein extracts separated by gel filtration showed that the low molecular weight nonprotein nitrogen compounds increased during aging. Results of nitrogen determinations of the gel filtered extracts also supported this finding. Data of ultraviolet scanning, vertical gel electrophoresis and two-dimensional paper chromatography-high voltage electrophoresis of gel filtration extracts suggested that the low molecular weight nonprotein nitrogen compounds were mostly nucleic acids. No evidence was obtained during the course of this study to indicate the presence of polypeptides in either the 0-day (fresh) or 12-day (aged) samples. Evidence was obtained which indicated that the extra protein was altered during 12 days of aging. Vertical gel electrophoretic patterns of the 0-day extra protein samples showed one more band than patterns of the 12-day samples. Disappearance of this band during aging might be the result of proteolysis or an alteration in the ability of the protein constituting this band to bind with other muscle proteins. The binding ability of this protein may be weakened during aging which would allow for it to be solubilized and removed during the extraction procedure of the extra protein. This may be an important finding when considering that changes in the binding and anchoring of proteins to the Z-line have been suggested by several workers as a partial explanation of the tenderization of meat during aging. Verification of the presence of tropomyosin and nucleoproteins in the extra protein complex was obtained by ultraviolet absorbance measurements and viscometric analysis of the extra protein fractions separated by vertical gel electrophoresis and collected by elution convection procedure.
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