Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1993-4-13
pubmed:databankReference
pubmed:abstractText
53 residues of the internal sequence from the proteinase-binding hen egg-white ovostatin have been determined. The stretch corresponds to residues 945-997 of human alpha 2-macroglobulin. The degree of conservation of residues of the two stretches is approx. 74%. Cys-949, being one constituent of the internal thiol ester site of members of the family of proteins related to alpha 2-macroglobulin, is an Asn-residue in hen egg-white ovostatin, but the other constituent, Gln-952, is preserved. The Cys-to-Asn substitution forms the chemical basis for the lack of thiol esters in hen egg-white ovostatin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
1162
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
230-2
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Evidence from sequence analysis that hen egg-white ovomacroglobulin (ovostatin) is devoid of an internal beta-Cys-gamma-Glu thiol ester.
pubmed:affiliation
Department of Molecular Biology, University of Arhus, Denmark.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't