A peptidase has been purified to near homogeneity from sheep red cells. This enzyme has a molecular weight of 340,000 and appears to contain six identical subunits. The enzyme is an endopeptidase of considerable specificity cleaving only bonds which are in hydrophobic regions of small peptides. The enzyme shows strong cooperativity in the hydrolysis of Gly-Ser-Ala but none in the hydrolysis of Gly-Met-Gly.
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Witheiler et al. (1972) studied this question.
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