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The Determination of Protease Specificity in Mouse Tissue Extracts by MALDI-TOF Mass Spectrometry: Manipulating PH to Cause Specificity Changes
Published on: May 25, 2018
Lysosomal proteinases in muscle tissue and leukocytes of meat animals
1Department of Food Science and Nutrition, University of Missouri-Columbia, Missouri, 65201, USA.
Abstract:
Carboxypeptidases A and B, cathepsins B, D and E, dipeptidyl aminopeptidase 1 and collagenase were extracted from bovine and porcine leukocyte lysosomes and diaphragm muscle lysosomes with 4% n-butyl alcohol in dry ice and various chemical properties were studied. The enzymes were classified by their specific activities with different substrates, pH optima, energies of activation and the influence of inhibitors and stimulators. Cathepsins D and E were the most active proteases studied and all enzymes were more active in leukocytes than in sediments from muscle tissue. The properties of these enzymes, compared with enzymes from other sources, and their possible involvement in meat tenderness are discussed.
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