Linked Life Data

11193401

Source:http://linkedlifedata.com/resource/pubmed/id/11193401

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2001-1-19
pubmed:abstractText
Transglutaminase activity was detected in suspensions of purified spores prepared from lysozyme-treated sporulating cells of Bacillus subtilis AJ 1307. The enzyme was easily solubilized from the spores upon incubation at pH 10.5 at 37 degrees C. The transglutaminase activity was separated into two fractions upon purification by hydrophobic interaction chromatography (TG1 and TG2). Each enzyme was purified to electrophoretic homogeneity (about 1,000-fold). Both enzymes had the same molecular weight of 29,000 as estimated by SDS-PAGE, had the same N-terminal 30 amino acid sequence, and also showed the same optimal temperature (60 degrees C) and pH (8.2). The purified enzyme catalyzed formation of cross-linked epsilon-(gamma-glutamyl)lysine isopeptides, resulting in the gel-formation of protein solutions such as alphas-casein and BSA.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0916-8451
pubmed:author
pubmed:issnType
Print
pubmed:volume
64
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2344-51
pubmed:dateRevised
2001-11-2
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Purification and characterization of novel transglutaminase from Bacillus subtilis spores.
pubmed:affiliation
Central Research Laboratories, Ajinomoto Co., Inc., Kawasaki, Kanagawa, Japan. shunichi_suzuki@ajinomoto.com
pubmed:publicationType
Journal Article