Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1985-12-24
pubmed:abstractText
In the bovine lens the gamma IV-crystallin fraction is a principal determinant of the phase separation and opacification temperature, Tc (Siezen et al, Proc. Natl. Acad. Sci. USA 82, 1985, 1701). We have now measured the effect on Tc of purified gamma IV-crystallin solutions produced by a variety of reagents which affect protein-protein, protein-water and water-water interactions. Ionic strengths less than physiological increase Tc dramatically, while higher ionic strength has very little effect. Calcium ion concentrations up to 8 mM produce no change in Tc. Glycerol and acrylamide both depress Tc linearly with reagent concentrations; Tc depression of gamma IV-crystallin by these compounds is quantitatively the same as for whole lens. Sulfhydryl reducing agents such as glutathione and dithiothreitol lower Tc, while hydrogen peroxide increases Tc. Changes in opacification temperature of gamma IV-crystallin produced by oxidizing and reducing agents are time-dependent and highly non-linear with reagent concentration. Our results clearly show that bovine gamma IV-crystallin is an important target protein for various reagents which are known perturbants of the opacification temperature of whole lens. The relevance of these findings to human diabetic and senile cataract formation is discussed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0271-3683
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1077-85
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Controlled modulation of the phase separation and opacification temperature of purified bovine gamma IV-crystallin.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.