Linked Life Data

3360754

Source:http://linkedlifedata.com/resource/pubmed/id/3360754

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1988-6-9
pubmed:abstractText
Trehalase solubilized with 0.5% Triton X-100 and 0.5% deoxycholate from the brush border membrane of rabbit kidney cortex was all adsorbed on phenyl-Sepharose equilibrated with elution buffer containing no detergents, and all the adsorbed enzyme was eluted in one peak on the addition of 0.5% Triton X-100 to the elution buffer, in contrast to the results reported by Nakano and Sacktor (J. Biochem. 97, 1329-1335 (1985], who separated two forms of trehalase differing in hydrophobicity from rabbit kidney. On concentration of detergent-solubilized extracts, followed by incubation at 37 degrees C, however, there appeared trehalase nonadsorbable on phenyl-Sepharose, i.e. a hydrophilic trehalase. Various protease inhibitors added to the concentrated extracts did not inhibit this conversion at all. The concentration-incubation treatment also increased the proportion of trehalase that interacts with Con A-Sepharose. These results indicate that kidney trehalase that interacts with Con A-Sepharose. These results indicate that kidney trehalase is susceptible to some lytic action of a factor(s) intrinsic to the brush border membrane (limited autolysis), as seen with rabbit intestinal trehalase (Yokota et al., (1986) Biochim. Biophys. Acta 881, 405-414). Therefore, in studies of the molecular form of trehalase (and other proteins) in the brush border membrane of the kidney and intestine where a lot of hydrolases exist, it is very important to take account of limited autolysis which results in some chemical modifications without affecting enzymatic activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
103
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
132-6
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
In vitro loss of hydrophobicity of trehalase from the brush border membrane of rabbit kidney cortex.
pubmed:affiliation
Research Institute of Environmental Medicine, Nagoya University, Aichi.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't