Linked Life Data

6630872

Source:http://linkedlifedata.com/resource/pubmed/id/6630872

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1983-12-20
pubmed:abstractText
Protein methylase II (S-adenosylmethionine:protein-carboxyl O-methyltransferase, EC. 2.1.1.24) which methyl esterifies free carboxyl groups of protein substrate using S-adenosyl-L-methionine as the methyl donor, has been purified from human erythrocytes approximately 13000-fold with a yield of 12%. The purified enzyme was over 95% pure as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. A bulk of hemoglobin present in the erythrocyte lysate, which severely limited the use of affinity chromatography for purification, was effectively removed by ammonium sulfate precipitation and by the subsequent salt washing of the precipitates followed by molecular sieve chromatography on Sephadex G-75. This preparation can be further purified by affinity chromatography, in which S-adenosyl-L-homocysteine is covalently linked to Sepharose-4B, followed by Sephadex G-75 chromatography to yield an enzyme with an activity of 27000 pmol methyl group transferred/mg/min at 37 degrees C.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0165-022X
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9-14
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Purification of protein methylase II from human erythrocytes.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.