Linked Life Data

2085958

Source:http://linkedlifedata.com/resource/pubmed/id/2085958

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1991-5-23
pubmed:abstractText
1. A chymotrypsinogen from pancreas of Japanese quail (Coturnix coturnix japonica) was purified by acid extraction, salt fractionation and chromatographic separation on CM-cellulose and Sephadex G-100, and gave a single protein band on SDS-PAGE. 2. Quail chymotrypsinogen had a mol. wt of 26,100 calculated from amino acid composition data, an isoelectric point of 7.68, a Km of 3.1 mM and K0 of 40.7 sec-1 for tyrosine ester substrate. 3. The activated chymotrypsinogen of quail had a maximum activity at pH 7.0-8.0 and at 45 degrees C, and was stable at pH 4.0-6.0 below 55 degrees C. 4. Comparison of quail and bovine chymotrypsinogens indicates that the activities of the enzymes from quail and bovine are more constant than their physical characteristics.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0305-0491
pubmed:author
pubmed:issnType
Print
pubmed:volume
97
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
761-6
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Purification and characterization of chymotrypsinogen from pancreas of Japanese quail (Coturnix coturnix japonica).
pubmed:affiliation
Department of Animal Science, Faculty of Agriculture, Kagoshima University, Japan.
pubmed:publicationType
Journal Article, Comparative Study