Premium
Partial Purification and Characterization of a Neutral Protease from Bovine Skeletal Muscle
Author(s) -
KANG C. K.,
DONNELLY T. H.,
JODLOWSKI R. F.,
WARNER W. D.
Publication year - 1981
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1981.tb15329.x
Subject(s) - protease , chemistry , chromatography , neutral protease , agarose , affinity chromatography , hydrolysis , size exclusion chromatography , calcium , myofibril , extraction (chemistry) , yield (engineering) , biochemistry , skeletal muscle , sepharose , phosphate , enzyme , biology , organic chemistry , materials science , metallurgy , endocrinology
A method has been developed for the partial purification of a calcium activated neutral protease from bovine muscle, since application of methods previously used for rabbit or porcine muscle gave little or no yield. The new method involves extraction with phosphate‐buffered KCl, saling out with (NH 4 ) 2 SO 4 , affinity chromatography on mercurial agarose followed by gel filtration. The bovine protease required calcium ion and reducing agent for activity with a pH optimum at 7.5 and hydrolyzed myofibrillar proteins.