Linked Life Data

11948558

Source:http://linkedlifedata.com/resource/pubmed/id/11948558

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2002-4-11
pubmed:abstractText
Modification of the enzyme alginate lyase (AL) with poly(ethylene glycol) (PEG) was attempted for the degradation and removal of alginate biofilms in infectious diseases. The modification of AL with PEG was attempted with three kinds of N-succinimidyl succinate PEG (SS-PEG), which differed in molecular weight (i.e., 2000, 5000 and 12,000 Da). The conjugation of PEG to free amino groups on AL was confirmed by gel permeation chromatography. Quantification of residual free amino groups revealed that PEG modification progressed further with a higher pH and a larger molar ratio of SS-PEG to AL. The reproducibility of the reaction was fairly good. The enzyme activity decreased with increasing PEG modification but the immunoreactivity toward anti-AL antibodies, as evaluated by an ELISA method, was much more remarkably reduced. The immunoreactivity was more reduced by the conjugated PEG with the larger molecular weight. In the reaction with PEG of molecular weight 12,000 Da, we obtained PEG-modified AL retaining approximately 40% enzyme activity but only 0.5% of the immunoreactivity of native AL.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0022-3549
pubmed:author
pubmed:copyrightInfo
Copyright 2002 Wiley-Liss, Inc. and the American Pharmaceutical Association J Pharm Sci 91:1191-1199, 2002
pubmed:issnType
Print
pubmed:volume
91
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1191-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Preparation and properties of alginate lyase modified with poly(ethylene glycol).
pubmed:affiliation
DDS Research Department, Discovery Research Laboratory, Tanabe Seiyaku Company, Ltd., 16-89, Kashima 3-chome, Yodogawa-ku, Osaka 532-8505, Japan. sakaki@dnavec.co.jp
pubmed:publicationType
Journal Article