Linked Life Data

21110915

Source:http://linkedlifedata.com/resource/pubmed/id/21110915

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2010-11-29
pubmed:abstractText
We report the tissue-specific distribution of chitinolytic activity in Korean ginseng root and characterize two 31-kDa chitinolytic enzymes. These two enzymes (SBF1 and SBF2) were purified 70- and 81-fold with yields of 0.75 and 1.25%, respectively, and exhibited optimal pH and temperature ranges of 5.0-5.5 and 40-50(o)C. With [(3)H]-chitin as a substrate, K(m) and V(max) values of SBF1 were 4.6 mM and 220 mmol/mg-protein/h, respectively, while those of SBF2 were 7.14 mM and 287 mmol/mg-protein/h. The purified enzymes showed markedly less activity with p-nitrophenyl-N-acetylglucosaminide and fluorescent 4-methylumbelliferyl glycosides of D-N-acetylglucosamine oligomers than with [(3)H]-chitin. End-product inhibition of both enzymes demonstrated that both are endochitinases with different N-acetylglucosaminidase activity. Furthermore, the NH(2)-terminal sequence of SBF1 showed a high degree of homology with other plant chitinases whereas the NH(2)-terminal amino acid of SBF2 was blocked. [BMB reports 2010; 43(11):726-731].
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1976-670X
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
726-31
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Distribution of chitinases and characterization of two chitinolytic enzymes from one-year-old Korean Ginseng (Panax ginseng C.A. Meyer) roots.
pubmed:affiliation
Department of Molecular Science and Technology, Graduate School, Ajou University, Suwon 442-749, Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't