Characterization of the human beta-crystallin gene Hu beta A3/A1 reveals ancestral relationships among the beta gamma-crystallin superfamily.
نویسندگان
چکیده
منابع مشابه
Congenital polymorphic cataract associated with a G to A splice site mutation in the human beta-crystallin gene CRYβA3/A1
PURPOSE To identify the underlying genetic defect in four generations of a Chinese family affected with bilateral congenital polymorphic cataracts. METHODS Family history and clinical data were recorded. The phenotype was documented using slit-lamp photography. Genomic DNA samples were extracted from peripheral blood of family members. Candidate genes were amplified using polymerase chain rea...
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Human betaB1-crystallin is a major eye-lens protein that undergoes in vivo truncation at the N-terminus with aging. By studying native betaB1 and truncated betaB1DeltaN41, which mimics an age-related in vivo truncation, we have determined quantitatively the effect of truncation on the oligomerization and phase transition properties of betaB1 aqueous solutions. The oligomerization studies show t...
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Aggregation of beta-lactoglobulin occurs mainly via intermolecular disulphide bond exchange. Upon heating, beta-lactoglobulin aggregated which increased with increasing pH. The presence of DTT led to more rapid aggregation and precipitation of beta-lactoglobulin. AlphaCrystallin prevented the aggregation of heat-stressed beta-lactoglobulin and was a more efficient chaperone at higher pH values....
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Objective(s) Resistance to the new generation of cephalosporins which is mediated by Extended-Spectrum beta-lactamases (ESBLs) has been found among Escherichia coli isolates throughout the world. These resistance genes and their producers, the micro-organisms carrying beta-lactamases, are responsible for serious clinical and therapeutic problems among inpatients and it is necessary to pay more...
متن کاملHuman alpha-crystallin. I. The isolation and characterization of newly synthesized alpha-crystallin.
Studies of the incorporation of 14C amino acids into human lens proteins demonstrate that an alpha-crystallin fraction takes up more than six times as much radioactivity as any other lens protein. Based on analyses with a calibrated Bio-Gel A-1.5 m column, a molecular weight of 4.9 x 10(5) +/- 5 per cent was obtained for this protein while sedimentation equilibrium analyses indicated a weight a...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1986
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)67257-6