Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1990-2-13
pubmed:abstractText
A protein inhibitor of locust gut alpha-amylase was purified from seeds of Job's Tears (Coix lachryma-jobi) using ammonium sulphate precipitation, affinity chromatography on Red Sepharose and reversed-phase HPLC. It consisted of two major isomers, each a dimer of two closely similar or identical subunits of Mr about 26,400, and associated by inter-chain disulphide bonds. These isomers also had closely similar amino acid compositions. The major isomer showed no inhibitory activity against amylases from other sources: human saliva, porcine pancreas, Bacillus subtilis, Aspergillus oryzae and barley malt. The manual DABITC/PITC method was used to determine about half of the amino acid sequence of the major isoform. This showed a high degree of homology with previously reported sequences of endochitinase enzymes from several species (tobacco, potato, barley, bean), and endochitinase activity was demonstrated by following the release of radioactivity from [3H]chitin. This novel combination of functions may be relevant to protection of the grain from insect feeding and fungal infection.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
999
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
260-6
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Purification and characterization of an insect alpha-amylase inhibitor/endochitinase from seeds of Job's Tears (Coix lachryma-jobi).
pubmed:affiliation
Biology Department, University of Durham, U.K.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't