Linked Life Data

7957177

Source:http://linkedlifedata.com/resource/pubmed/id/7957177

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-11-28
pubmed:abstractText
A transglutaminase (pTGase) was purified from filarial nematode, Brugia malayi. The steps used for purification were thermoprecipitation, ammonium sulfate precipitation, gel filtration on Superose 12 HR 10/30, ion-exchange chromatography on a Mono-Q column and further gel filtration on Superose 12 HR 10/30. The last step yielded an electrophoretically homogenous enzyme protein with 2200-fold purification and a reproducible yield of approximately 20%. The purified enzyme had a molecular mass of 56 kDa, specific activity of 2.25 U/mg protein and an isoelectric point of 7.2. The enzyme was active in the basic pH range with an optimum activity at pH 8.5. The pTGase activity was Ca(2+)-dependent and was inhibited by ammonia, primary amines, EDTA, and -SH group blocking reagents. The enzyme activity was also inhibited by high salt (NaCl and KCl) concentrations, detergents, metal ions, and organic solvents. Ampholine (pH 6-8) at 1% (by vol.) caused about 20% inhibition of pTGase activity but at 3% (by vol.) the inhibition increased up to 80%. Similarly, the micromolar concentrations of GTP inhibited the enzyme activity only moderately but at millimolar concentration a significant inhibition was observed. The stability of the pTGase was not affected by 0.1% SDS or other physical parameters such as freezing and thawing. Further, the pTGase was found to be highly thermostable (stable at 60 degrees C for several hours) with optimum activity observed at 55 degrees C. The distinct substrate specificity, unique N-terminal sequence along with the other physico-chemical properties studied, suggested that pTGase is a novel member of transglutaminase family.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
225
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
625-34
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Purification and characterization of a novel transglutaminase from filarial nematode Brugia malayi.
pubmed:affiliation
Department of Clinical Investigation, University of Texas, M.D. Anderson Cancer Center, Houston.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't