Isolation and Purification of Active Proteases from Sheep Abomasum and Their Biological Activity
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Sheep abomasum active proteases (SAPs) were purified by chromatography over a column of Sephadex G-25 and by ultrafiltration. The SAPs were found to contain proteases of molecular mass 14 kDa and active peptides with molecular masses varying in the range 651.39–4248.08 Da. Peptide fractions of SAPs reduced significantly (up to 72.0 ± 2.3% inhibition) accumulation of malondialdehyde (MDA) in brain homogenate of laboratory rats.
Keywordssheep abomasum (SA) peptide extraction and isolation electrophoresis liquid-chromatography–massspectrometry analysis sheep abomasum active proteases (SAPs) proteolytic activity antioxidant activity lipid peroxidation (LPO) malondialdehyde (MDA)
We thank the Central Asian Drug Research and Development Center of the Chinese Academy of Sciences and the Training Project of Xinjiang Autonomous Region for Technological Innovations of Youth Talents for financial support.