Show simple item record

dc.contributor.authorLusk, William Earlen_US
dc.date.accessioned2013-01-24T14:37:41Z
dc.date.available2013-01-24T14:37:41Z
dc.date.issued1950
dc.date.submitted1950
dc.identifier.otherb14733894
dc.identifier.urihttps://hdl.handle.net/2144/4781
dc.descriptionThesis (M.A.)--Boston Universityen_US
dc.description.abstractLysozymic activity may be broken down into three phases: (1) adsorbtion of the enzyme onto the cell surface containing an acetylated aminopolysaccharide; (2) depolymerization of the substrate; and (3) visible alteration of the cell (37). During adsorption the electrokinetic potential rises on a sensitive cell, and then falls to normal. On an insensitive cell the reverse process occurs (21). Cells are lysed in an unimolecular reaction (87). The substrate then changes into N-acetylaminohexose or ketose, and after a series of chemical and physical changes visible lysis occurs, and the cell contents are liberated.en_US
dc.language.isoen_US
dc.publisherBoston Universityen_US
dc.rightsBased on investigation of the BU Libraries' staff, this work is free of known copyright restrictionsen_US
dc.titleA comparison of Lysozyme with bacterial hyaluronidaseen_US
dc.typeThesis/Dissertationen_US
etd.degree.nameMaster of Artsen_US
etd.degree.levelmastersen_US
etd.degree.disciplineBiochemistryen_US
etd.degree.grantorBoston Universityen_US


This item appears in the following Collection(s)

Show simple item record