Linked Life Data

7763795

Source:http://linkedlifedata.com/resource/pubmed/id/7763795

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-8-24
pubmed:abstractText
In the 60% ethanol extract of soybean seeds, a prominent protein band was visible after polyacrylamide gel electrophoresis, which had a molecular weight of about 55 x 10(3) M(r). This protein was purified to homogeneity by buffered ethanol extraction and preparatory gel electrophoresis. Since the N-terminus was apparently blocked, the protein was cleaved with cyanogen bromide and the largest fragment was isolated and a partial sequence determined. The sequence of the 27 N-terminal amino acid residues matched a published soybean beta-amylase peptide sequence. In addition, the purified protein had a high specific activity for beta-amylase and was not a glycoprotein. Furthermore, the partial sequence (106 nucleotides) of a cDNA clone, isolated from a soybean seed cDNA library by antibody screening, matched the cDNA sequence of soybean beta-amylase except for one base. Therefore, the ethanol-soluble protein was identified as beta-amylase. The enzyme was purified to homogeneity using a two-step purification procedure with a yield of over 50%.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
B
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0031-9422
pubmed:author
pubmed:issnType
Print
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
535-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Identification of an ethanol-soluble protein as beta-amylase and its purification from soybean seeds.
pubmed:affiliation
Section of Plant Biology, Cornell University, Ithaca, NY 14853.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't