Linked Life Data

16663912

Source:http://linkedlifedata.com/resource/pubmed/id/16663912

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2010-6-29
pubmed:abstractText
The lipase from the scutella of corn (Zea mays) MO-17 seedlings was purified 272-fold to apparent homogeneity as evidenced by sodium dodecyl sulfate polyacrylamide gel electrophoresis and double immunodiffusion. The procedure involved isolation of the lipid bodies, extraction with diethyl ether, DE-52 ion exchange chromatography, and sucrose density gradient centrifugation. The enzyme had an approximate molecular weight of 270,000 daltons after sucrose density gradient centrifugation, and 65,000 daltons after sodium dodecyl sulfate polyacrylamide gel electrophoresis. The lipase contained no cysteine and its molecular weight in sodium dodecyl sulfate was not reduced by beta-mercaptoethanol. The amino acid composition as well as a biphasic partition using Triton X-114 revealed the enzyme to be a hydrophobic protein. Rabbit gamma-globulin containing antibodies raised against the purified lipase formed one precipitin line with the lipase in a double diffusion test, and precipitated all the lipase activity from a solution.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:month
Nov
pubmed:issn
0032-0889
pubmed:author
pubmed:issnType
Print
pubmed:volume
76
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
719-22
pubmed:dateRevised
2010-9-15
pubmed:year
1984
pubmed:articleTitle
Purification and initial characterization of lipase from the scutella of corn seedlings.
pubmed:affiliation
Biology Department, University of South Carolina, Columbia, South Carolina 29208.
pubmed:publicationType
Journal Article