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Can J Biochem ; 53(3): 269-74, 1975 Mar.
Article in English | MEDLINE | ID: mdl-1125813

ABSTRACT

The acid protease produced by a strain of Mucor miehei isolated in Cuba was purified by column electrofocusing and partially characterized as to amino-acid composition, molecular weight, helical content, total carbohydrate content, and approximate isoelectric point; A detailed comparison of these results was reported previously for Mucor miehei protease (Ottesen, M. & Rickert, W;S. (1970) C.R. Trav. Labmcarlsberg 37, 301) suggested that the two enzymes are similar but not identicalmthis conclusion was reinforced by an analysis of circular-dichroism spectra.


Subject(s)
Mucor/enzymology , Peptide Hydrolases , Amino Acids/analysis , Carbohydrates/analysis , Circular Dichroism , Cuba , Isoelectric Focusing , Peptide Hydrolases/isolation & purification , Peptide Hydrolases/metabolism , Protein Conformation , Spectrophotometry, Ultraviolet
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