Calf rennet lysozyme

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State: Public
Version: author
Serval ID
serval:BIB_477DAE170CF0
Type
Inproceedings: an article in a conference proceedings.
Publication sub-type
Abstract (Abstract): shot summary in a article that contain essentials elements presented during a scientific conference, lecture or from a poster.
Collection
Publications
Title
Calf rennet lysozyme
Title of the conference
12th annual meeting of the Union of Swiss societies of experimental biology
Author(s)
Pahud J.J., Schwarz K., Meyer I., Widmer F.
Address
Basel, Switzerland, March 13-14, 1980
ISBN
0014-4754
Publication state
Published
Issued date
1980
Peer-reviewed
Oui
Volume
36
Series
Experientia
Pages
729
Language
english
Abstract
A strong lytic activity against Micrococcus lysodeikticus cell walls was detected in calf rennet. Purification was carried out using ion exchange, electrofocusing and gel-filtration. Hydrolysis of the bacterial peptidoglycan by the isolated enzyme released only reducing groups, thus indicating true glycolytic activity. Comparative tests with hen egg white lysozyme suggested a similar mode of action. - Multiple enzyme forms were revealed, with mol.wts of ca. 15,000, pH optima of ca. 5.0, and pl's ranging from 6.5 to 7.8. The enzyme exhibited remarkable stability against heat and pH conditions ranging from 2 to 9. Significant chitinase activity was observed at pH 5.0. - Specifie antisera revealed sharp precipitation arcs in the ß- to y-electrophoretic region, when diffused against the most acidic or basic molecular forms, respectively. - The rennet enzyme differs markedly from the bovine milk lysozyme described only by Chaudan et al. (BBA 110, 389, 1965).
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13/08/2015 8:53
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20/08/2019 14:53
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