FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2059310462> ?p ?o ?g. }

• W2059310462 endingPage "6225" @default.
• W2059310462 startingPage "6220" @default.
• W2059310462 abstract "Human and other mammalian lens proteins are composed of three major crystallins: α-, β-, and γ-crystallin. α-Crystallin plays a prominent role in the supramolecular assembly required to maintain lens transparency. With age, the crystallins, especially α-crystallin, undergo posttranslational modifications that may disrupt the supramolecular assembly, and the lens becomes susceptible to other stresses resulting in cataract formation. Because these modifications occur even at a relatively young age, it is difficult to obtain pure, unmodified crystallins for in vitro experiments. α-Crystallin is composed of two subunits, αA and αB. Before the application of recombinant DNA technology, these two α-crystallin subunits were separated from calf lens in the denatured state and reconstituted by the removal of the denaturant, but they were not refolded properly. In the present studies, we applied the recombinant DNA technology to prepare native, unmodified αA- and αB-crystallins for conformational and functional studies. The expressed proteins from Escherichia coli are in the native state and can be studied directly. First, αA and αB cDNAs were isolated from a human lens epithelial cell cDNA library. The cDNAs were cloned into a pAED4 expression vector and then expressed in E. coli strain BL21(DE3). Pure recombinant αA- and αB-crystallins were obtained after purification by gel filtration and DEAE liquid chromatography. They were subjected to conformational studies involving various spectroscopic measurements and an assessment of chaperone-like activity. αA- and αB-crystallins have not only different secondary structure, but also tertiary structure. 1-Anilino-8-naphthalene sulfonate fluorescence indicates that αB-crystallin is more hydrophobic than αA-crystallin. The chaperone-like activity, as measured by the ability to protect insulin aggregation, is about 4 times greater for αB- than for αA-crystallin. The resulting data provide a base line for further studies of human lens α-crystallin. Human and other mammalian lens proteins are composed of three major crystallins: α-, β-, and γ-crystallin. α-Crystallin plays a prominent role in the supramolecular assembly required to maintain lens transparency. With age, the crystallins, especially α-crystallin, undergo posttranslational modifications that may disrupt the supramolecular assembly, and the lens becomes susceptible to other stresses resulting in cataract formation. Because these modifications occur even at a relatively young age, it is difficult to obtain pure, unmodified crystallins for in vitro experiments. α-Crystallin is composed of two subunits, αA and αB. Before the application of recombinant DNA technology, these two α-crystallin subunits were separated from calf lens in the denatured state and reconstituted by the removal of the denaturant, but they were not refolded properly. In the present studies, we applied the recombinant DNA technology to prepare native, unmodified αA- and αB-crystallins for conformational and functional studies. The expressed proteins from Escherichia coli are in the native state and can be studied directly. First, αA and αB cDNAs were isolated from a human lens epithelial cell cDNA library. The cDNAs were cloned into a pAED4 expression vector and then expressed in E. coli strain BL21(DE3). Pure recombinant αA- and αB-crystallins were obtained after purification by gel filtration and DEAE liquid chromatography. They were subjected to conformational studies involving various spectroscopic measurements and an assessment of chaperone-like activity. αA- and αB-crystallins have not only different secondary structure, but also tertiary structure. 1-Anilino-8-naphthalene sulfonate fluorescence indicates that αB-crystallin is more hydrophobic than αA-crystallin. The chaperone-like activity, as measured by the ability to protect insulin aggregation, is about 4 times greater for αB- than for αA-crystallin. The resulting data provide a base line for further studies of human lens α-crystallin." @default.
• W2059310462 created "2016-06-24" @default.
• W2059310462 creator A5015265146 @default.
• W2059310462 creator A5048234916 @default.
• W2059310462 creator A5061691596 @default.
• W2059310462 date "1997-03-01" @default.
• W2059310462 modified "2023-10-01" @default.
• W2059310462 title "Conformational and Functional Differences between Recombinant Human Lens αA- and αB-Crystallin" @default.
• W2059310462 cites W1538223857 @default.
• W2059310462 cites W1564205457 @default.
• W2059310462 cites W1592971775 @default.
• W2059310462 cites W1966594754 @default.
• W2059310462 cites W1968663827 @default.
• W2059310462 cites W1968802798 @default.
• W2059310462 cites W1974471144 @default.
• W2059310462 cites W1981337104 @default.
• W2059310462 cites W1984837082 @default.
• W2059310462 cites W1985515623 @default.
• W2059310462 cites W1998134951 @default.
• W2059310462 cites W1998495384 @default.
• W2059310462 cites W1999145875 @default.
• W2059310462 cites W2006791133 @default.
• W2059310462 cites W2007950936 @default.
• W2059310462 cites W2016433029 @default.
• W2059310462 cites W2019804051 @default.
• W2059310462 cites W2033123702 @default.
• W2059310462 cites W2039873895 @default.
• W2059310462 cites W2044031095 @default.
• W2059310462 cites W2044881463 @default.
• W2059310462 cites W2045683458 @default.
• W2059310462 cites W2046253402 @default.
• W2059310462 cites W2051066123 @default.
• W2059310462 cites W2053081081 @default.
• W2059310462 cites W2056301348 @default.
• W2059310462 cites W2077392023 @default.
• W2059310462 cites W2100837269 @default.
• W2059310462 cites W2110336102 @default.
• W2059310462 cites W2124330908 @default.
• W2059310462 cites W2162735744 @default.
• W2059310462 cites W4232534952 @default.
• W2059310462 doi "https://doi.org/10.1074/jbc.272.10.6220" @default.
• W2059310462 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9045637" @default.
• W2059310462 hasPublicationYear "1997" @default.
• W2059310462 type Work @default.
• W2059310462 sameAs 2059310462 @default.
• W2059310462 citedByCount "155" @default.
• W2059310462 countsByYear W20593104622012 @default.
• W2059310462 countsByYear W20593104622013 @default.
• W2059310462 countsByYear W20593104622014 @default.
• W2059310462 countsByYear W20593104622015 @default.
• W2059310462 countsByYear W20593104622016 @default.
• W2059310462 countsByYear W20593104622017 @default.
• W2059310462 countsByYear W20593104622018 @default.
• W2059310462 countsByYear W20593104622019 @default.
• W2059310462 countsByYear W20593104622020 @default.
• W2059310462 countsByYear W20593104622021 @default.
• W2059310462 countsByYear W20593104622022 @default.
• W2059310462 countsByYear W20593104622023 @default.
• W2059310462 crossrefType "journal-article" @default.
• W2059310462 hasAuthorship W2059310462A5015265146 @default.
• W2059310462 hasAuthorship W2059310462A5048234916 @default.
• W2059310462 hasAuthorship W2059310462A5061691596 @default.
• W2059310462 hasBestOaLocation W20593104621 @default.
• W2059310462 hasConcept C104317684 @default.
• W2059310462 hasConcept C12554922 @default.
• W2059310462 hasConcept C142724271 @default.
• W2059310462 hasConcept C153911025 @default.
• W2059310462 hasConcept C185592680 @default.
• W2059310462 hasConcept C187882448 @default.
• W2059310462 hasConcept C2775962898 @default.
• W2059310462 hasConcept C40767141 @default.
• W2059310462 hasConcept C547475151 @default.
• W2059310462 hasConcept C55493867 @default.
• W2059310462 hasConcept C71924100 @default.
• W2059310462 hasConcept C7263354 @default.
• W2059310462 hasConcept C86803240 @default.
• W2059310462 hasConceptScore W2059310462C104317684 @default.
• W2059310462 hasConceptScore W2059310462C12554922 @default.
• W2059310462 hasConceptScore W2059310462C142724271 @default.
• W2059310462 hasConceptScore W2059310462C153911025 @default.
• W2059310462 hasConceptScore W2059310462C185592680 @default.
• W2059310462 hasConceptScore W2059310462C187882448 @default.
• W2059310462 hasConceptScore W2059310462C2775962898 @default.
• W2059310462 hasConceptScore W2059310462C40767141 @default.
• W2059310462 hasConceptScore W2059310462C547475151 @default.
• W2059310462 hasConceptScore W2059310462C55493867 @default.
• W2059310462 hasConceptScore W2059310462C71924100 @default.
• W2059310462 hasConceptScore W2059310462C7263354 @default.
• W2059310462 hasConceptScore W2059310462C86803240 @default.
• W2059310462 hasIssue "10" @default.
• W2059310462 hasLocation W20593104621 @default.
• W2059310462 hasOpenAccess W2059310462 @default.
• W2059310462 hasPrimaryLocation W20593104621 @default.
• W2059310462 hasRelatedWork W2338137066 @default.
• W2059310462 hasRelatedWork W2350146650 @default.
• W2059310462 hasRelatedWork W2363249581 @default.
• W2059310462 hasRelatedWork W2373690171 @default.
• W2059310462 hasRelatedWork W2376921901 @default.

• next