Linked Life Data

1126947

Source:http://linkedlifedata.com/resource/pubmed/id/1126947

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1975-8-11
pubmed:abstractText
Acinetobacter glutaminase-asparaginase was chemically modified by succinylation and glycosylation with glycopeptides from human fibrin and gamma-globulin. These modifications markedly prolonged the half-lives of the enzyme in mice, rats, and rabbits. The plasma half-life in mice increased with decreasing isoelectric point. Glycosylation caused greater prolongation in rodents than succinylation. The kinetic properties of the modified enzymes were unchanged. Succinylation protected the enzyme from trypsin digestion. Glycosylated preparations had less heat inactivation than native and succinylated enzyme. Sedimentation equilibrium studies on a succinylated preparation showed reversible dissociation to a dimer (71, 400 g/mol) with an association constant of 1.3 times 10-6 liters/mol. This dissociation was identical with native enzyme, except for a 3% increase in molecular weight due to succinate groups. Sedimentation equilibrium studies on glycosylated preparations showed mixtures of molecular weight from 60, 000 to over 180, 000. Gel filtration and active enzyme sedimentation showed active polymers, but no active species smaller than tetramer.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
250
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4165-70
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
Biologic and physical properties of succinylated and glycosylated Acinetobacter glutaminase-asparaginase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.