Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1995-2-2
pubmed:abstractText
All three fish antifreeze protein types (I, II and III) inhibit the growth of ice to form hexagonal bipyramidal ice crystals of characteristic morphology. Mixtures of these different antifreezes produced ice crystals of hybrid shapes and dimensions, consistent with the different antifreeze types binding to the same ice surfaces. The activity of the mixtures was independent of the proportions of the iso-active antifreeze protein stocks present, indicating that the different antifreezes neither attenuated nor potentiated each other's activity. We suggest that antifreeze protein molecules are independently active and do not require protein-protein interactions for ice-binding.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
357
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
183-6
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Mixing antifreeze protein types changes ice crystal morphology without affecting antifreeze activity.
pubmed:affiliation
Department of Biochemistry, Queen's University, Kingston, Ont., Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't