Linked Life Data

16657241

Source:http://linkedlifedata.com/resource/pubmed/id/16657241

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2010-6-29
pubmed:abstractText
While the total amount of proteolytic enzyme activity in the latex from Ficus carica varieties Kadota and Black Mission showed seasonal variation and was different between the 2 crops of figs in the latex collected at the same time and from the same tree, there is no difference in the number of multiple molecular forms of ficin present as demonstrated by chromatography on carboxymethyl-cellulose. The number of multiple forms of ficin is also the same, with 1 exception, among samples of latex which have been collected with no protection against proteolysis, samples which have been collected directly into sodium p-chloromercuribenzoate to inhibit all proteolysis and samples which have been held at an elevated temperature so as to encourage proteolysis. Evidence is presented to support the proposal that component C of Ficus carica variety Kadota is not present in the original latex but that it is produced from component D during the purification procedure. The data support the hypothesis that, with the possible exception of 1 component, the multiple molecular forms of ficin are not the result of artifacts produced by autolysis during collection, storage and purification of the sample.
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
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1560-5
pubmed:dateRevised
2010-9-15
pubmed:year
1969
pubmed:articleTitle
Multiple molecular forms of ficin-evidence against autolysis as explanation.
pubmed:affiliation
Department of Food Science and Technology, University of California, Davis, California 95616.
pubmed:publicationType
Journal Article