Linked Life Data

6093779

Source:http://linkedlifedata.com/resource/pubmed/id/6093779

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1984-12-12
pubmed:abstractText
Evidence is presented on the existence of an acid phosphoprotein phosphatase (APPase) associated with rat splenic cell nucleoli. The enzyme is purified 1250-fold from 0.3 M NaCl nucleolar extract by means of chromatography on P cellulose and Sephacryl S-200. The nucleolar acid phosphoprotein phosphatase is a very basic protein (pI 8.3) and shows maximal activity at pH 5.8. It dephosphorylates acidic phosphoproteins (casein and phosvitin), ATP, and p-nitrophenyl phosphate, but not basic phosphoproteins (histones and protamine phosphate). The enzyme activity is very dependent on reducing agents, especially on ascorbic acid. Divalent and monovalent cations did not affect phosphatase activity, but heavier divalent metals, Co2+ and Zn2+, strongly inhibit the enzyme activity. The activity was also inhibited by N-ethylmaleimide, indicating a requirement for free sulfhydryl groups. The estimated molecular weight of the purified enzyme is approximately 38,000 by gel filtration and sedimentation in sucrose gradient concentration.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-2944
pubmed:author
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
88-98
pubmed:dateRevised
2009-11-11
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Characterization of low-molecular-weight acid phosphoprotein phosphatase associated with rat splenic cell nucleoli.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't