Linked Life Data

12595722

Source:http://linkedlifedata.com/resource/pubmed/id/12595722

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 3
pubmed:dateCreated
2003-2-21
pubmed:abstractText
AaV-SP-I and AaV-SP-II, two glycosylated serine proteinases from Agkistrodon acutus venom with fibrinogenolysis and esterolysis activities, have been purified to homogeneity by three-step ion-exchange chromatography. Estimated by SDS-PAGE, the molecular weights of AaV-SP-I and AaV-SP-II are about 32 and 31 kDa under reducing conditions and 26 and 25 kDa under non-reducing conditions, respectively. The first 24 N-terminal amino-acid residues are the same in both sequences and display a high homology with those of several snake-venom serine proteinases. However, the proteins possess obviously distinct carbohydrate contents. Using the conventional hanging-drop vapour-diffusion method, single crystals of both enzymes were grown that were suitable for X-ray diffraction analysis. The crystals of AaV-SP-I and AaV-SP-II belong to space groups P2(1)2(1)2(1) and C2, respectively. In each case there is only one molecule in the asymmetric unit.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
59
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
547-50
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Purification, N-terminal sequencing, partial characterization, crystallization and preliminary crystallographic analysis of two glycosylated serine proteinases from Agkistrodon acutus venom.
pubmed:affiliation
Key Laboratory of Structural Biology, Chinese Academy of Sciences, School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't