Accession Number : AD0682392

Title :   STUDIES ON CELLULOLYTIC ENZYMES. V. SOME STRUCTURAL PROPERTIES OF THE CELLULASE FROM PENICILLIUM NOTATUM,

Corporate Author : SVENSKA TRAFORSKNINGSINSTITUTET STOCKHOLM

Personal Author(s) : Eriksson,Karl-Erik ; Pettersson,Goeran

Report Date : 11 JUL 1967

Pagination or Media Count : 5

Abstract : Mercuric ions were found to strongly inhibit cellulolytic activity. The activity could be restored by cysteine as well as by chloride ions. By difference spectrophotometric methods the mercuric ions could be shown to interact with tryptophanyl groups of the enzyme. Electrolytic reduction showed that the disulfide bridge, present in the enzyme, was essential for the activity. The cellulase molecule was not attacked by exopeptidases under nondenaturating conditions, but treatment with endopeptidases caused a pronounced decrease in activity. Active fragments could not be obtained with endopeptidases. (Author)

Descriptors :   (*ENZYMES, *PENICILLIUM(PENICILLINS)), CELLS(BIOLOGY), ORGANIC SULFUR COMPOUNDS, CHEMICAL ANALYSIS, PEPTIDE HYDROLASES, TRYPTOPHAN, IONS, MERCURY, CHLORIDES, SWEDEN, CHEMICAL PROPERTIES

Subject Categories : Biochemistry

Distribution Statement : APPROVED FOR PUBLIC RELEASE