Linked Life Data

8951044

Source:http://linkedlifedata.com/resource/pubmed/id/8951044

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-1-16
pubmed:abstractText
A poly(ADP-ribose) glycohydrolase was purified more than 5,000-fold to apparent homogeneity from pig testis nuclei with a yield of 16%. A protein band, whose molecular mass (Mr) was estimated to be 58,000, detected by SDS-polyacrylamide gel electrophoresis of the purified preparation, was shown to have glycohydrolase activity upon assay by the renaturation method. A native Mr of 51,000 was determined by gel permeation. This polypeptide is a basic protein with a pI value of 8.8. The mode of hydrolysis of poly(ADP-ribose) [(ADP-ribose)n] by this enzyme is exoglycosidic, yielding ADP-ribose as the final product. The Km value for (ADP-ribose)n (average chain length, n = 15) is 5.4 microM and the Vmax of its hydrolysis is 34.5 micromol x min(-1) x mg protein(-1). The optimum pH for enzyme activity is 7.2. Low concentrations (50 approximately 150 mM) of monovalent salts stimulate the enzyme activity. The poly(ADP-ribose) glycohydrolase present in pig testis nuclei has some properties different from either nuclear poly(ADP-ribose) glycohydrolase (type I) or cytoplasmic poly(ADP-ribose) glycohydrolase (type II), purified previously from several tissues including pig thymus, guinea pig liver, calf thymus, human erythrocytes, and placenta. These differences suggest the tissue specificity of poly(ADP-ribose) glycohydrolase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
336
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
139-46
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Properties of poly(ADP-ribose) glycohydrolase purified from pig testis nuclei.
pubmed:affiliation
Department of Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
pubmed:publicationType
Journal Article